Structure of PDB 2q2o Chain A

Receptor sequence
>2q2oA (length=307) Species: 1423 (Bacillus subtilis) [Search protein sequence]
KKMGLLVMAYGTPYKEEDIERYYTHIRRGRKPEPEMLQDLKDRYEAIGGI
SPLAQITEQQAHNLEQHLNEIQDEITFKAYIGLKHIEPFIEDAVAEMHKD
GITEAVSIVLAPHFSTFSVQSYNKRAKEEAEKLGGLTITSVESWYDEPKF
VTYWVDRVKETYASMPEDERENAMLIVSACSLPEKIKEFGDPYPDQLHES
AKLIAEGAGVSEYAVGWQSEGNTPDPWLGPDVQDLTRDLFEQKGYQAFVY
VPVGFVADHLEVLYDNDYECKVVTDDIGASYYRPEMPNAKPEFIDALATV
VLKKLGR
3D structure
PDB2q2o Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y13 I29 P35 K87 H88 C183 D261 E264 D268
Catalytic site (residue number reindexed from 1) Y10 I26 P32 K84 H85 C180 D258 E261 D265
Enzyme Commision number 4.99.1.9: coproporphyrin ferrochelatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 H01 A Y13 I29 R30 R31 R33 F120 L185 G224 N225 T226 W230 Y10 I26 R27 R28 R30 F117 L182 G221 N222 T223 W227
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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Cellular Component
External links
PDB RCSB:2q2o, PDBe:2q2o, PDBj:2q2o
PDBsum2q2o
PubMed18423489
UniProtP32396|CPFC_BACSU Coproporphyrin III ferrochelatase (Gene Name=cpfC)

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