Structure of PDB 1q9i Chain A

Receptor sequence
>1q9iA (length=568) Species: 56812 (Shewanella frigidimarina) [Search protein sequence]
ADNLAEFHVQNQECDSCHTPDGELSNDSLTYENTQCVSCHGTLAEVAETT
KHEHYNAHASHFPGEVACTSCHSAHEKSMVYCDSCHSFDFNMPYAKKWLR
DEPTIAELAKDKSERQAALASAPHDTVDVVVVGSGGAGFSAAISATDSGA
KVILIEKEPVIGGNAKLAAGGMNAAWTDQQKAKKITDSPELMFEDTMKGG
QNINDPALVKVLSSHSKDSVDWMTAMGADLTDVGMMGGASVNRAHRPTGG
CGVGAHVVQVLYDNAVKRNIDLRMNTRGIEVLKDDKGTVKGILVKGMYKG
YYWVKADAVILATGGFAKNNERVAKLDPSLKGFISTNQPGAVGDGLDVAE
NAGGALKDMQYIQAHPTLSVKGGVMVTEAVRGNGAILVNREGKRFVNEIT
TRDKASAAILAQTGKSAYLIFDDSVRKSLCKIDKYIGLGVAPTADSLVKL
GKMEGIDGKALTETVARYNSLVSSGKDTDFERPNLPRALNEGNYYAIEVT
PGVHHTMGGVMIDTKAEVMNAKKQVIPGLYGAGEVTGGVHGANRLGGNAI
SDIITFGRLAGEEAAKYS
3D structure
PDB1q9i Probing Domain Mobility in a Flavocytochrome
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M236 Q363 H365 M375 E378 R381 R402 H504 H505 R544
Catalytic site (residue number reindexed from 1) M236 Q363 H365 M375 E378 R381 R402 H504 H505 R544
Enzyme Commision number 1.3.2.4: fumarate reductase (cytochrome).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0008202 steroid metabolic process
Cellular Component
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:1q9i, PDBe:1q9i, PDBj:1q9i
PDBsum1q9i
PubMed15109257
UniProtQ07WU7|FCCA_SHEFN Fumarate reductase (cytochrome) (Gene Name=fccA)

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