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Crystal structure of C-src SH3 domain without atcun motif: monomer 2

Analyse Crystal structure of C-src SH3 domain without atcun motif: monomer 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6XVM
Type
protein
Length
237 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proto-oncogene tyrosine-protein kinase src
EC
2.7.10.2
UniProt
P00523
Pockets
2 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 3% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)protein595% helix, 42% strandP00523
BProto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)protein580% helix, 41% strandP00523
C, DProto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)protein605% helix, 42% strandP00523

Ligands and binding sites

  • GOL · Glycerol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14410.670.7966empty
2500.320.7814empty

Interfaces

3 interfaces between chains.

  • B–C · 372 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 318 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 304 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6XVM · Crystal structure of c-Src SH3 domain without ATCUN motif: monomer 2 · the same entry in another collection · chain A against A, TM-score 1.00

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