MolNFT v1 · #112817 · protein

Crystal structure of aminotransferase ATMS13 from actinomadura melliaura

4ZWV · Putative aminotransferase: “Crystal structure of aminotransferase ATMS13 from actinomadura melliaura”. X-ray diffraction, 9 pockets (best druggability 0.76). MolNFT v1 #112817 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4ZWV
Type: protein
Length: 740 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative aminotransferase
UniProt: Q0H2X1
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative aminotransferase	protein	370	41% helix, 17% strand	Q0H2X1

Ligands and binding sites

GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	94	0.76	0.97	30	empty
2	63	0.73	0.99	22	empty
3	263	0.63	0.81	45	empty
4	231	0.57	0.78	31	empty
5	153	0.37	0.72	35	empty

Interfaces

1 interface between chains.

A–B · 2560 Å² buried · 38 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered, cofactor).

Compared structures

4ZWV · Crystal Structure of Aminotransferase AtmS13 from Actinomadura melliaura · 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 Q0H2X1
Elsewhere: RCSB PDB 4ZWV · PDBe 4ZWV · UniProt Q0H2X1

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