MolNFT v1 · #135102 · protein

Crystal structure of aat H143L:H189L double mutant

5TOT · Aspartate aminotransferase, cytoplasmic: “Crystal structure of aat H143L:H189L double mutant”. X-ray diffraction, 10 pockets (best druggability 0.71). MolNFT v1 #135102 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5TOT
Type: protein
Length: 811 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate aminotransferase, cytoplasmic
EC: 2.6.1.1, 2.6.1.3
UniProt: P00503
Pockets: 10 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartate aminotransferase, cytoplasmic (EC 2.6.1.1, 2.6.1.3)	protein	414	46% helix, 13% strand	P00503
B	Aspartate aminotransferase, cytoplasmic (EC 2.6.1.1, 2.6.1.3)	protein	397	44% helix, 14% strand	P00503

Pockets

10 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	137	0.71	0.91	28	empty
2	678	0.71	0.78	70	empty
3	151	0.57	0.82	28	empty
4	115	0.50	0.80	16	empty
5	102	0.40	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 3352 Å² buried · 57 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

P00503 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase, cytoplasmic (P00503) · 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 P00503
Elsewhere: RCSB PDB 5TOT · PDBe 5TOT · UniProt P00503

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