MolNFT v1 · #18812 · protein

Crystal structure of homoprotocatechuate 2,3-dioxygenase from brevibacterium fuscum (full length protein)

1Q0O: “Crystal structure of homoprotocatechuate 2,3-dioxygenase from brevibacterium fuscum (full length protein)”. X-ray diffraction, 1 ligand (FE), 3 pockets (best druggability 0.85). MolNFT v1 #18812 on GenesisL1: 3D structure, binding…

PDB: 1Q0O
Type: protein
Length: 712 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homoprotocatechuate 2,3-dioxygenase
EC: 1.13.11.15
UniProt: Q45135
Ligands: FE
Pockets: 3 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Homoprotocatechuate 2,3-dioxygenase (EC 1.13.11.15)	protein	356	18% helix, 34% strand	Q45135

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	609	0.85	0.90	67	empty
2	64	0.38	0.79	16	empty
3	52	0.38	0.80	15	empty

Interfaces

1 interface between chains.

A–B · 1702 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

1Q0O · Crystal structure of homoprotocatechuate 2,3-dioxygenase from brevibacterium fuscum (full… · 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 Q45135
Elsewhere: RCSB PDB 1Q0O · PDBe 1Q0O · UniProt Q45135

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