Macromolecule Content
Unique protein chains: 2
Display Files
Download Files
YAP65 WW domain complexed to Acetyl-PLPPY
DOI: 10.2210/pdb1k9r/pdb
Classification:
Deposited:
Deposition author(s):
,&,&,&,&,&,&,&,&
Mutation(s):
Structural Biology Knowledgebase:
Experimental Data Snapshot
SOLUTION NMR
Conformers Calculated: 200
Conformers Submitted: 20
Selection Criteria:
Structures with the Lowest Energy
wwPDB Validation report is not available for this NMR entry.
Classification:
Total Structure Weight:
Show All Chains
Macromolecule Entities
Toggle Protein Feature View
Show All Entities
Show First Few Entities
65 kDa Yes-associated protein
Fragment: Wild type WW domain
Find similar proteins by: Sequence | Structure&
Protein Feature View - UniProtKB AC:
WW domain binding protein-1
Fragment: residues 149-153
Mutation: P47L
Modified Residues 1 Unique
2D Diagram
NON-POLYMER
Experimental Data
SOLUTION NMR
Conformers Calculated: 200
Conformers Submitted: 20
Selection Criteria: structures with the lowest energy
Structure Validation
Validation report is not available for this NMR entry.
Deposition Data
Deposited Date:
Released Date:
Deposition author(s):
Pires, J.R., Taha-Nejad, F., Toepert, F., Ast, T., Hoffmuller, U., Schneider-Mergener, J., Kuhne, R., Macias, M.J., Oschkinat, H.
Revision History
Type: Other | Details: Remove PRD info on PRD molecule with WAIT status
Type: Other | Details: Add PRD info
Type: Version format compliance | Details: compliance with PDB Exchange Dictionary V4
The RCSB PDB () is managed by two members of the Research Collaboratory for Structural Bioinformatics:
RCSB PDB is a member of theProtein Symmetry: Asymmetric ()
Protein Stoichiometry: Monomer
Macromolecule Content
Unique protein chains: 1
Display Files
Download Files
Bacillus ciruclans strain 251 Cyclodextrin glycosyl transferase mutant G179L
DOI: 10.2210/pdb1kcl/pdb
Classification:
Deposited:
Deposition author(s):
Expression System:
Escherichia coli
Mutation(s):
Structural Biology Knowledgebase:
Experimental Data Snapshot
X-RAY DIFFRACTION
Resolution: 1.94
R-Value Free: 0.190
R-Value Work: 0.171
wwPDB Validation
Classification:
Total Structure Weight:
Show All Chains
Macromolecule Entities
Toggle Protein Feature View
Show All Entities
Show First Few Entities
Cyclodextrin glycosyltransferase
Mutation: G179L
Find similar proteins by: Sequence | Structure&
Protein Feature View - UniProtKB AC:
Ligands 5 Unique
Name / Formula / InChI Key
2D Diagram & Interactions
3D Interactions
C12 H22 O11
GUBGYTABKSRVRQ-ASMJPISFSA-N
Black dashed lines indicate hydrogen bonds, salt bridges, and metal interactions. Green solid line show hydrophobic interactions and green dashed lines show π-π and π-cation interactions.
Source Information
Interactions are determined by geometric criteria as described in K. Stierand, M. Rarey (2010),
Drawing the PDB: Protein-ligand complexes in two dimensions, ACS Med. Chem. Lett., DOI:
Ions and some metal complexes are excluded, as well as cases where no
interaction profile could be generated. Poseview diagrams can be calculated
for approximately 92% of the remaining complexes in the PDB.
is developed at the
Center for Bioinformatics Hamburg
and jointly provided with
as a community service at the PDB.
is provided by BioSolveIT.
ALPHA-D-GLUCOSE
WQZGKKKJIJFFOK-DVKNGEFBSA-N
Black dashed lines indicate hydrogen bonds, salt bridges, and metal interactions. Green solid line show hydrophobic interactions and green dashed lines show π-π and π-cation interactions.
Source Information
Interactions are determined by geometric criteria as described in K. Stierand, M. Rarey (2010),
Drawing the PDB: Protein-ligand complexes in two dimensions, ACS Med. Chem. Lett., DOI:
Ions and some metal complexes are excluded, as well as cases where no
interaction profile could be generated. Poseview diagrams can be calculated
for approximately 92% of the remaining complexes in the PDB.
is developed at the
Center for Bioinformatics Hamburg
and jointly provided with
as a community service at the PDB.
is provided by BioSolveIT.
BETA-D-GLUCOSE
WQZGKKKJIJFFOK-VFUOTHLCSA-N
Black dashed lines indicate hydrogen bonds, salt bridges, and metal interactions. Green solid line show hydrophobic interactions and green dashed lines show π-π and π-cation interactions.
Source Information
Interactions are determined by geometric criteria as described in K. Stierand, M. Rarey (2010),
Drawing the PDB: Protein-ligand complexes in two dimensions, ACS Med. Chem. Lett., DOI:
Ions and some metal complexes are excluded, as well as cases where no
interaction profile could be generated. Poseview diagrams can be calculated
for approximately 92% of the remaining complexes in the PDB.
is developed at the
Center for Bioinformatics Hamburg
and jointly provided with
as a community service at the PDB.
is provided by BioSolveIT.
(4S)-2-METHYL-2,4-PENTANEDIOL
SVTBMSDMJJWYQN-YFKPBYRVSA-N
Black dashed lines indicate hydrogen bonds, salt bridges, and metal interactions. Green solid line show hydrophobic interactions and green dashed lines show π-π and π-cation interactions.
Source Information
Interactions are determined by geometric criteria as described in K. Stierand, M. Rarey (2010),
Drawing the PDB: Protein-ligand complexes in two dimensions, ACS Med. Chem. Lett., DOI:
Ions and some metal complexes are excluded, as well as cases where no
interaction profile could be generated. Poseview diagrams can be calculated
for approximately 92% of the remaining complexes in the PDB.
is developed at the
Center for Bioinformatics Hamburg
and jointly provided with
as a community service at the PDB.
is provided by BioSolveIT.
CALCIUM ION
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Black dashed lines indicate hydrogen bonds, salt bridges, and metal interactions. Green solid line show hydrophobic interactions and green dashed lines show π-π and π-cation interactions.
Source Information
Interactions are determined by geometric criteria as described in K. Stierand, M. Rarey (2010),
Drawing the PDB: Protein-ligand complexes in two dimensions, ACS Med. Chem. Lett., DOI:
Ions and some metal complexes are excluded, as well as cases where no
interaction profile could be generated. Poseview diagrams can be calculated
for approximately 92% of the remaining complexes in the PDB.
is developed at the
Center for Bioinformatics Hamburg
and jointly provided with
as a community service at the PDB.
is provided by BioSolveIT.
Experimental Data
X-RAY DIFFRACTION
Resolution: 1.94 &A
R-Value Free: 0.190
R-Value Work: 0.171
Space Group:
Electron Density Server:
Unit Cell:
Length (&A)
a = 114.71
b = 109.47
Structure Validation
Deposition Data
Deposited Date:
Released Date:
Deposition author(s):
Rozeboom, H.J., Uitdehaag, J.C.M., Dijkstra, B.W.
Revision History
Type: Version format compliance | Details: compliance with PDB Exchange Dictionary V4
The RCSB PDB () is managed by two members of the Research Collaboratory for Structural Bioinformatics:
RCSB PDB is a member of theProtein Symmetry: Asymmetric ()
Protein Stoichiometry: Monomer
Protein Symmetry: C1 ()
Protein Stoichiometry: A
Macromolecule Content
Unique protein chains: 1
Display Files
Download Files
Src Thr338Ile inhibited in the DFG-Asp-Out conformation
DOI: 10.2210/pdb3g6h/pdb
Classification:
Deposited:
Deposition author(s):
,&,&,&,&,&,&,&
Expression System:
Escherichia coli
Mutation(s):
Structural Biology Knowledgebase:
Experimental Data Snapshot
X-RAY DIFFRACTION
Resolution: 2.35
R-Value Free: 0.283
R-Value Work: 0.225
wwPDB Validation
Classification:
Total Structure Weight:
Show All Chains
Macromolecule Entities
Toggle Protein Feature View
Show All Entities
Show First Few Entities
Proto-oncogene tyrosine-protein kinase Src
Fragment: Protein kinase Domain
Mutation: T338I
Find similar proteins by: Sequence | Structure&
Protein Feature View - UniProtKB AC:
Ligands 1 Unique
Name / Formula / InChI Key
2D Diagram & Interactions
3D Interactions
N-{4-methyl-3-[(3-{4-[(3,4,5-trimethoxyphenyl)amino]- 1,3,5-triazin-2-yl}pyridin-2-yl)amino]phenyl}- 3-(trifluoromethyl)benzamide
C32 H28 F3 N7 O4
SNOVXGXKOHJZJH-UHFFFAOYSA-N
Black dashed lines indicate hydrogen bonds, salt bridges, and metal interactions. Green solid line show hydrophobic interactions and green dashed lines show π-π and π-cation interactions.
Source Information
Interactions are determined by geometric criteria as described in K. Stierand, M. Rarey (2010),
Drawing the PDB: Protein-ligand complexes in two dimensions, ACS Med. Chem. Lett., DOI:
Ions and some metal complexes are excluded, as well as cases where no
interaction profile could be generated. Poseview diagrams can be calculated
for approximately 92% of the remaining complexes in the PDB.
is developed at the
Center for Bioinformatics Hamburg
and jointly provided with
as a community service at the PDB.
is provided by BioSolveIT.
External Ligand Annotations
Binding Affinity (Sequence Identity %)
N/A in BindingDB
Experimental Data
X-RAY DIFFRACTION
Resolution: 2.35 &A
R-Value Free: 0.283
R-Value Work: 0.225
Space Group:
Electron Density Server:
Unit Cell:
Length (&A)
& = 100.99
Structure Validation
Deposition Data
Deposited Date:
Released Date:
Deposition author(s):
Seeliger, M.A., Ranjitkar, P., Kasap, C., Shan, Y., Shaw, D.E., Shah, N.P., Kuriyan, J., Maly, D.J.
Revision History
Type: Version format compliance | Details: compliance with PDB Exchange Dictionary V4
The RCSB PDB () is managed by two members of the Research Collaboratory for Structural Bioinformatics:
RCSB PDB is a member of the}