MolNFT v1 · #134181 · protein

C-src V281C kinase domain in complex with rao-IV-151

5SWH · Proto-oncogene tyrosine-protein kinase src: “C-src V281C kinase domain in complex with rao-IV-151”. X-ray diffraction, 1 ligand (71D), 3 pockets (best druggability 0.74). MolNFT v1 #134181 on GenesisL1: 3D structure, binding sites…

PDB: 5SWH
Type: protein
Length: 519 residues
Chains: 2
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
Ligands: 71D
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)	protein	258	40% helix, 15% strand	P00523
B	Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)	protein	261	39% helix, 15% strand	P00523

Ligands and binding sites

71D · (2R)-3-[4-amino-5-(4-chlorophenyl)-7-(2-methoxyethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]-2-cyano-N-(propan-2-yl)propanamide · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	995	0.74	0.77	93	71D
2	287	0.61	0.79	31	71D
3	114	0.36	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 364 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

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 P00523
Elsewhere: RCSB PDB 5SWH · PDBe 5SWH · UniProt P00523

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