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Crystal structure of a prolyl 4-hydroxylase complexed with alpha- ketoglutarate from the pathogenic bacterium bacillus anthracis in C2221

Analyse Crystal structure of a prolyl 4-hydroxylase complexed with alpha- ketoglutarate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HV4
Type: protein
Length: 193 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2OG-FE(II) oxygenase
UniProt: Q81LZ8
Ligands: AKG, K, CD
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2OG-FE(II) oxygenase	protein	193	23% helix, 33% strand	Q81LZ8

Ligands and binding sites

AKG · 2-oxoglutaric acid · ligand · chains A
K · Potassium ion · metal · 6 copies · chains A
CD · Cadmium ion · metal · 5 copies · chains A

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

Pockets

2 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	66	0.69	0.95	19	CD, AKG
2	60	0.31	0.76	13	empty

Compared structures

5HV4 · Crystal Structure of a Prolyl 4-Hydroxylase Complexed with Alpha-ketoglutarate from the… · 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 Q81LZ8
Elsewhere: RCSB PDB 5HV4 · PDBe 5HV4 · UniProt Q81LZ8

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