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Structure of aminotransferase-substrate complex

Analyse Structure of aminotransferase-substrate complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VO1
Type: protein
Length: 904 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 454AA long hypothetical 4-aminobutyrate aminotransferase
UniProt: O50131
Ligands: PGU
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	454AA long hypothetical 4-aminobutyrate aminotransferase	protein	452	40% helix, 18% strand	O50131

Ligands and binding sites

PGU · N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid · ligand · 2 copies · chains A, B

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

Pockets

8 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	428	0.77	0.86	69	PGU
2	350	0.76	0.87	53	PGU
3	137	0.51	0.80	24	empty
4	87	0.34	0.74	18	empty
5	82	0.34	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 5197 Å² buried · 83 hydrogen bonds · protein-protein

Compared structures

7VO1 · Structure of aminotransferase-substrate complex · 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 O50131
Elsewhere: RCSB PDB 7VO1 · PDBe 7VO1 · UniProt O50131

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