Structure of PDB 5hv0 Chain B Binding Site BS01

Receptor Information

>5hv0 Chain B (length=197) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

NNNQIGENKEQTIFDHKGNVIKTEDREIQIISKFEEPLIVVLGNVLSDEE
CDELIELSKSKLSGAFLDDNELTAKIEKRISSIMNVPASHGEGLHILNYE
VDQQYKAHYDYFAEHSRSAANNRISTLVMYLNDVEEGGETFFPKLNLSVH
PRKGMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTYK

Ligand information

Ligand ID

InChI

InChI=1S/Cd/q+2

InChIKey

WLZRMCYVCSSEQC-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341	[Cd++]
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Cd+2]

Formula

Name

CADMIUM ION

ChEMBL

DrugBank

ZINC

PDB chain

5hv0 Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	5hv0 Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis.
Resolution	1.63 Å
Binding residue (original residue number in PDB)	H127 D129 H193
Binding residue (residue number reindexed from 1)	H108 D110 H174
Annotation score	1

Enzymatic activity

Enzyme Commision number

Gene Ontology

	Molecular Function
GO:0003674	molecular_function
GO:0004656	procollagen-proline 4-dioxygenase activity
GO:0005506	iron ion binding
GO:0016705	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0031418	L-ascorbic acid binding
GO:0046872	metal ion binding
GO:0051213	dioxygenase activity

	Biological Process
GO:0008150	biological_process
GO:0018401	peptidyl-proline hydroxylation to 4-hydroxy-L-proline

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Molecular Function

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Biological Process

External links

PDB	RCSB:5hv0, PDBe:5hv0, PDBj:5hv0
PDBsum	5hv0
PubMed	27139630
UniProt	A0A4Y1WAP5

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