Structure of PDB 5iav Chain B Binding Site BS01

Receptor Information

>5iav Chain B (length=194) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

EQTIFDHKGNVIKTEDREIQIISKFEEPLIVVLGNVLSDEECDELIELSK
SKLARSKVGSGAFLDDNELTAKIEKRISSIMNVPASHGEGLHILNYEVDQ
QYKAHYDYFAEHSRSAANNRISTLVMYLNDVEEGGETFFPKLNLSVHPRK
GMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTYK

Ligand information

Ligand ID

InChI

InChI=1S/Co/q+2

InChIKey

XLJKHNWPARRRJB-UHFFFAOYSA-N

SMILES

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

Formula

Name

COBALT (II) ION

PDB chain

5iav 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	5iav Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.
Resolution	1.7 Å
Binding residue (original residue number in PDB)	H127 D129 H193
Binding residue (residue number reindexed from 1)	H105 D107 H171
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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Biological Process

External links

PDB	RCSB:5iav, PDBe:5iav, PDBj:5iav
PDBsum	5iav
PubMed	27129244
UniProt	A0A4Y1WAP5

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