MolNFT v1 · #32600 · protein

Crystal structure of the human P21-activated kinase 4

2BVA: “Crystal structure of the human P21-activated kinase 4”. X-ray diffraction, 8 pockets (best druggability 0.62). MolNFT v1 #32600 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2BVA
Type: protein
Length: 548 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P21-activated kinase 4
EC: 2.7.1.37
UniProt: Q8NCH5
Pockets: 8 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P21-activated kinase 4 (EC 2.7.1.37)	protein	273	37% helix, 9% strand	Q8NCH5
B	P21-activated kinase 4 (EC 2.7.1.37)	protein	275	36% helix, 12% strand	Q8NCH5

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.62	0.78	53	empty
2	251	0.60	0.79	33	empty
3	189	0.56	0.80	31	empty
4	181	0.53	0.78	27	empty
5	167	0.47	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 454 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

2BVA · Crystal structure of the human P21-activated kinase 4 · 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 Q8NCH5
Elsewhere: RCSB PDB 2BVA · PDBe 2BVA · UniProt Q8NCH5

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