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Crystal structure of human tyrosine-protein kinase C-src, in complex with AMP-pnp

Analyse Crystal structure of human tyrosine-protein kinase C-src, in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2SRC
Type: protein
Length: 450 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase src
EC: 2.7.1.112
UniProt: P12931
Ligands: ANP
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase src (EC 2.7.1.112)	protein	450	28% helix, 23% strand	P12931

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	471	0.75	0.83	58	ANP
2	913	0.70	0.75	80	empty
3	298	0.52	0.74	31	empty
4	64	0.35	0.77	16	empty
5	63	0.33	0.76	16	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

2SRC · Crystal structure of human tyrosine-protein kinase C-src, in complex with AMP-pnp · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P12931
Elsewhere: RCSB PDB 2SRC · PDBe 2SRC · UniProt P12931

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