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Aspartate aminotransferase, H-asp complex, closed conformation

Analyse Aspartate aminotransferase, H-asp complex, closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OXP
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate aminotransferase
EC: 2.6.1.1
UniProt: P00508
Ligands: IK2
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartate aminotransferase (EC 2.6.1.1)	protein	401	46% helix, 14% strand	P00508

Ligands and binding sites

IK2 · 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

3 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	254	0.63	0.81	44	IK2
2	233	0.54	0.77	25	empty
3	111	0.44	0.77	14	empty

Compared structures

1OXP · Aspartate aminotransferase, H-asp complex, closed conformation · the same entry in another collection · chain A against A, TM-score 1.00
P00508 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase, mitochondrial (P00508) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P00508
Elsewhere: RCSB PDB 1OXP · PDBe 1OXP · UniProt P00508

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