Structure of PDB 3m4z Chain A Binding Site BS01
Receptor Information
>3m4z Chain A (length=309) Species:
1423
(Bacillus subtilis) [
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SRKKMGLLVMAYGTPYKEEDIERYYTHIRRGRKPEPEMLQDLKDRYEAIG
GISPLAQITEQQAHNLEQHLNEIQDEITFKAYIGLKHIEPFIEDAVAEMH
KDGITEAVSIVLAPHFSTFSVQSYNKRAKEEAEKLGGLTITSVESWYDEP
KFVTYWVDRVKETYASMPEDERENAMLIVSAHSLPEKIKEFGDPYPDQLH
ESAKLIAEGAGVSEYAVGWQSEGNTPDPWLGPDVQDLTRDLFEQKGYQAF
VYVPVGFVADHLEVLYDNDYECKVVTDDIGASYYRPEMPNAKPEFIDALA
TVVLKKLGR
Ligand information
Ligand ID
CO
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
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
3m4z Chain A Residue 310 [
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Receptor-Ligand Complex Structure
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PDB
3m4z
Bacterial ferrochelatase goes human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase
Resolution
1.94 Å
Binding residue
(original residue number in PDB)
H182 E263
Binding residue
(residue number reindexed from 1)
H182 E263
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
Y12 I28 P34 K86 H87 H182 D260 E263 D267
Catalytic site (residue number reindexed from 1)
Y12 I28 P34 K86 H87 H182 D260 E263 D267
Enzyme Commision number
4.99.1.9
: coproporphyrin ferrochelatase.
Gene Ontology
Molecular Function
GO:0004325
ferrochelatase activity
GO:0016829
lyase activity
GO:0046872
metal ion binding
Biological Process
GO:0006783
heme biosynthetic process
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3m4z
,
PDBe:3m4z
,
PDBj:3m4z
PDBsum
3m4z
PubMed
UniProt
P32396
|CPFC_BACSU Coproporphyrin III ferrochelatase (Gene Name=cpfC)
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