Structure of PDB 1ffv Chain B

Receptor sequence

>1ffvB (length=797) Species: 47421 (Hydrogenophaga pseudoflava) [Search protein sequence]

DAEARELALAGMGASRLRKEDARFIQGKGNYVDDIKMPGMLHMDIVRAPI
AHGRIKKIHKDAALAMPGVHAVLTAEDLKPLKLHWMPTLAGDVAAVLADE
KVHFQMQEVAIVIADDRYIAADAVEAVKVEYDELPVVIDPIDALKPDAPV
LREDLAGKTSGAHGPREHHNHIFTWGAGDKAATDAVFANAPVTVSQHMYY
PRVHPCPLETCGCVASFDPIKGDLTTYITSQAPHVVRTVVSMLSGIPESK
VRIVSPDIGGGFGNKVGIYPGYVCAIVASIVLGRPVKWVEDRVENISTTA
FARDYHMDGELAATPDGKILGLRVNVVADHGAFDACADPTKFPAGLFHIC
SGSYDIPRAHCSVKGVYTNKAPGGVAYRCSFRVTEAVYLIERMVDVLAQK
LNMDKAEIRAKNFIRKEQFPYTTQFGFEYDSGDYHTALKKVLDAVDYPAL
RAEQAARRADPNSPTLMGIGLVTFTEVVGAGPSKMCDILGVGMFDSCEIR
IHPTGSAIARMGTITQGQGHQTTYAQIIATELGIPSEVIQVEEGDTSTAP
YGLGTYGSRSTPVAGAAIALAARKIHAKARKIAAHMLEVNENDLDWEVDR
FKVKGDDSKFKTMADIAWQAYHQPPAGLEPGLEAVHYYDPPNFTYPFGIY
LCVVDIDRATGETKVRRFYALDDCGTRINPMIIEGQIHGGLTEGYAVAMG
QQMPFDAQGNLLGNTLMDYFLPTAVETPHWETDHTVTPSPHHPIGAKGVA
ESPHVGSIPTFTAAVVDAFAHVGVTHLDMPHTSYRVWKSLKEHNLAL

3D structure

PDB

1ffv The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.

Chain

Resolution

2.25 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Q237 V272 P349 I355 R384 C385 E757 S758
Catalytic site (residue number reindexed from 1)	Q231 V266 P343 I349 R378 C379 E751 S752
Enzyme Commision number	1.2.5.3: aerobic carbon monoxide dehydrogenase.

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	PCD	B	G266 G267 F268 G269 A382 X384 X385 Q522 G523 Q524 H526 T529 Y562 G563 S564 S566 T567 C680 I684 I689 Q692 K753 G754 V755 A756 E757	G260 G261 F262 G263 A376 X378 X379 Q516 G517 Q518 H520 T523 Y556 G557 S558 S560 T561 C674 I678 I683 Q686 K747 G748 V749 A750 E751

Gene Ontology

	Molecular Function
GO:0005506	iron ion binding
GO:0005507	copper ion binding
GO:0008805	carbon-monoxide oxygenase activity
GO:0016491	oxidoreductase activity
GO:0030151	molybdenum ion binding
GO:0043885	anaerobic carbon-monoxide dehydrogenase activity
GO:0046872	metal ion binding

View graph for
Molecular Function

External links

PDB	RCSB:1ffv, PDBe:1ffv, PDBj:1ffv
PDBsum	1ffv
PubMed	10966817
UniProt	P19913\|DCML_HYDPS Carbon monoxide dehydrogenase large chain (Gene Name=cutL)

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