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Crystal structure of an aspartate aminotransferase from pseudomonas

Analyse Crystal structure of an aspartate aminotransferase from pseudomonas in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TI8
Type: protein
Length: 771 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminotransferase
UniProt: W5IS25
Ligands: CA
Pockets: 8 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminotransferase	protein	387	44% helix, 20% strand	W5IS25
B	Aminotransferase	protein	384	45% helix, 20% strand	W5IS25

Ligands and binding sites

CA · Calcium ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	745	0.71	0.78	72	empty
2	461	0.68	0.79	50	empty
3	75	0.35	0.76	21	empty
4	82	0.34	0.75	17	empty
5	67	0.33	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 2412 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5TI8 · Crystal Structure of an aspartate aminotransferase from Pseudomonas · the same entry in another collection · chain B against B, 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 W5IS25
Elsewhere: RCSB PDB 5TI8 · PDBe 5TI8 · UniProt W5IS25

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