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2,3-dihydroxybenzoate decarboxylase of aspergillus oryzae

Analyse 2,3-dihydroxybenzoate decarboxylase of aspergillus oryzae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A19
Type: protein
Length: 678 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidohydrolase 2
UniProt: A0A1S9DW14
Ligands: MG
Pockets: 10 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Amidohydrolase 2	protein	339	55% helix, 13% strand	A0A1S9DW14

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.63	0.93	17	empty
2	90	0.56	0.85	21	empty
3	124	0.54	0.82	35	empty
4	98	0.53	0.84	22	empty
5	105	0.52	0.83	21	empty

Interfaces

1 interface between chains.

A–B · 730 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

7A19 · 2,3-Dihydroxybenzoate Decarboxylase of Aspergillus oryzae · 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 A0A1S9DW14
Elsewhere: RCSB PDB 7A19 · PDBe 7A19 · UniProt A0A1S9DW14

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