Structure of PDB 1qni Chain F

Receptor sequence
>1qniF (length=572) Species: 2743 (Marinobacter nauticus) [Search protein sequence]
AHVAPGELDEYYGFWSGGHQGEVRVLGVPSMRELMRIPVFNVDSATGWGI
TNESKEILGGDQQYLNGDCHHPHISMTDGRYDGKYLFINDKANTRVARIR
LDIMKTDKITHIPNVQAIHGLRLQKVPKTNYVFCNAEFVIPQPNDGTDFS
LDNSYTMFTAIDAETMDVAWQVIVDGNLDNTDADYTGKYATSTCYNSERA
VDLAGTMRNDRDWVVVFNVERIAAAVKAGNFKTIGDSKVPVVDGRGESEF
TRYIPVPKNPHGLNTSPDGKYFIANGKLSPTVSVIAIDKLDDLFEDKIEL
RDTIVAEPELGLGPLHTTFDGRGNAYTTLFIDSQVCKWNIADAIKHYNGD
RVNYIRQKLDVQYQPGHNHASLTESRDADGKWLVVLSKFSKDRFLPVGPL
HPENDQLIDISGEEMKLVHDGPTYAEPHDCILVRRDQIKTKKIYERNDPY
FASCRAQAEKDGVTLESDNKVIRDGNKVRVYMTSVAPQYGMTDFKVKEGD
EVTVYITNLDMVEDVTHGFCMVNHGVSMEISPQQTASVTFTAGKPGVYWY
YCNWFCHALHMEMVGRMLVEAA
3D structure
PDB1qni A novel type of catalytic copper cluster in nitrous oxide reductase.
ChainF
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V494 P496
Catalytic site (residue number reindexed from 1) V485 P487
Enzyme Commision number ?
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 CUA F H526 C561 W563 C565 H569 M572 H517 C552 W554 C556 H560 M563
BS02 CA F Y204 E207 T215 D221 N268 Y195 E198 T206 D212 N259
BS03 CA F K397 E412 K388 E403
Gene Ontology
Molecular Function
GO:0004129 cytochrome-c oxidase activity
GO:0005507 copper ion binding
GO:0005509 calcium ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050304 nitrous-oxide reductase activity
Biological Process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0016020 membrane
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qni, PDBe:1qni, PDBj:1qni
PDBsum1qni
PubMed10700275
UniProtQ7SIA3

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