Structure of PDB 1jry Chain A

Receptor sequence
>1jryA (length=568) Species: 56812 (Shewanella frigidimarina) [Search protein sequence]
ADNLAEFHVQNQECDSCHTPDGELSNDSLTYENTQCVSCHGTLAEVAETT
KHEHYNAHASHFPGEVACTSCHSAHEKSMVYCDSCHSFDFNMPYAKKWLR
DEPTIAELAKDKSERQAALASAPHDTVDVVVVGSGGAGFSAAISATDSGA
KVILIEKEPVIGGNAKLAAGGMNAAWTDQQKAKKITDSPELMFEDTMKGG
QNINDPALVKVLSSHSKDSVDWMTAMGADLTDVGMMGGASVNRAHRPTGG
AGVGAHVVQVLYDNAVKRNIDLRMNTRGIEVLKDDKGTVKGILVKGMYKG
YYWVKADAVILATGGFAKNNERVAKLDPSLKGFISTNQPGAVGDGLDVAE
NAGGALKDMQYIQAHPTLSVKGGVMVTEAVRGNGAILVNREGKRFVNEIT
TKDKASAAILAQTGKSAYLIFDDSVRKSLSKIDKYIGLGVAPTADSLVKL
GKMEGIDGKALTETVARYNSLVSSGKDTDFERPNLPRALNEGNYYAIEVT
PGVHHTMGGVMIDTKAEVMNAKKQVIPGLYGAGEVTGGVHGANRLGGNAI
SDIITFGRLAGEEAAKYS
3D structure
PDB1jry Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase.
ChainA
Resolution2.0 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 K402 H504 H505 R544
Catalytic site (residue number reindexed from 1) M236 Q363 H365 M375 E378 R381 K402 H504 H505 R544
Enzyme Commision number 1.3.2.4: fumarate reductase (cytochrome).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0009055 electron transfer activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0008202 steroid metabolic process
GO:0009061 anaerobic respiration
GO:0019645 anaerobic electron transport chain
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
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:1jry, PDBe:1jry, PDBj:1jry
PDBsum1jry
PubMed11591148
UniProtP0C278|FCCA_SHEFR Fumarate reductase (cytochrome) (Gene Name=fccA)

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