MolNFT v1 · #24606 · protein

Crystal structure of the T198A mutant of PFPK5

1V0B · Cell division control protein 2 homolog: “Crystal structure of the T198A mutant of PFPK5”. X-ray diffraction, 11 pockets (best druggability 0.70). MolNFT v1 #24606 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1V0B
Type: protein
Length: 547 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division control protein 2 homolog
EC: 2.7.1.-
UniProt: Q07785
Pockets: 11 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division control protein 2 homolog (EC 2.7.1.-)	protein	286	40% helix, 14% strand	Q07785
B	Cell division control protein 2 homolog (EC 2.7.1.-)	protein	261	38% helix, 16% strand	Q07785

Pockets

11 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	186	0.70	0.88	26	empty
2	200	0.67	0.85	25	empty
3	150	0.53	0.80	25	empty
4	62	0.42	0.81	16	empty
5	96	0.38	0.76	20	empty

Compared structures

1V0B · Crystal structure of the t198a mutant of pfpk5 · the same entry in another collection · chain A against A, TM-score 1.00
Q07785 · AlphaFold monomer V2.0 prediction for cell division control protein 2 homolog (Q07785) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q07785
Elsewhere: RCSB PDB 1V0B · PDBe 1V0B · UniProt Q07785

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