Research workbench

Aspartate aminotransferase P195A mutant

Analyse Aspartate aminotransferase P195A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BQA
Type: protein
Length: 792 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate aminotransferase
EC: 2.6.1.1
UniProt: P00509
Pockets: 10 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aspartate aminotransferase (EC 2.6.1.1)	protein	396	47% helix, 14% strand	P00509

Pockets

10 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	577	0.70	0.79	55	empty
2	532	0.69	0.79	48	empty
3	60	0.38	0.80	20	empty
4	55	0.36	0.79	15	empty
5	61	0.34	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 3177 Å² buried · 61 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

1BQA · Aspartate aminotransferase P195A mutant · the same entry in another collection · chain B against B, TM-score 1.00
P00509 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase (P00509) · 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 P00509
Elsewhere: RCSB PDB 1BQA · PDBe 1BQA · UniProt P00509

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