MolNFT v1 · #124059 · protein

Structural characterisation of fold IV-transaminase, CPUTA1, from curtobacterium pusillum

5K3W: “Structural characterisation of fold IV-transaminase, CPUTA1, from curtobacterium pusillum”. X-ray diffraction, 2 ligands (PLP, GAB), 4 pockets (best druggability 0.82). MolNFT v1 #124059 on GenesisL1: 3D structure, binding sites and…

PDB: 5K3W
Type: protein
Length: 588 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CPUTA1
Ligands: PLP, GAB
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CPUTA1	protein	298	32% helix, 30% strand	—
B	CPUTA1	protein	290	30% helix, 30% strand	—

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
GAB · 3-aminobenzoic acid · ligand · chains A

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

Pockets

4 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	731	0.82	0.86	93	PLP
2	453	0.70	0.81	49	PLP
3	76	0.33	0.75	16	empty
4	55	0.28	0.74	23	empty

Interfaces

1 interface between chains.

A–B · 2357 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

5K3W · Structural characterisation of fold IV-transaminase, CpuTA1, from Curtobacterium pusillum · 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
Elsewhere: RCSB PDB 5K3W · PDBe 5K3W

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