Structure of PDB 5xmj Chain A

Receptor sequence
>5xmjA (length=622) Species: 879 (Megalodesulfovibrio gigas) [Search protein sequence]
MQIYHTDVLCIGGALAGERVAVEASMAGLKTIMLSLVPPRRSHSSAAQGG
MQAALGNAIMGDGDSPDVHFADTVKGSDWGCDQEVARIFADTAPIVMREV
AHWGVPWNRVVPGKHTYYKGGKPFEAEEKAEKAGLIHARAFGGTAAWRTC
YTADGTGRSVLNTLDTKCLQYGVTVHDRMQAEALIHDGGNCLGCIARCLR
TGELVAYLATSTLIATGGYGRIYKATTNAVICDGGGQIIALDTGLVPMGN
MEAVQFHPTGTVPTDILVTEGCRGDGGTLLDVNQYRFMPDYEPDKAQLAS
RDVVSRRMTEHMRKGLGVKSPYGDHLWLDIRHLGEKHITTKLREVYDICT
NFLGVNPIHQLIPVRPTHHYSMGGVRTNRDGAAYGLKGLFSAGESACWDM
HGFNRLGGNSLAETVVAGRYIGERMVEFTKGATPSFGMQYVEDAHKKVQE
RITDIVTGRKGKENTFKIRDEMHDIMMEGVGIFRNGTDLQKAVNKLEELY
DRSQKISLSSACKGMNPELSTALRIRGMLKLAQCTAYGALDRTESRGAHT
REDFPERNDKEWLNRTLSYWKEGASMPTLEYEEASPYYEMPPGDRGYGGG
VTIANELPPEKFVIPEAAKENL
3D structure
PDB5xmj Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas.
ChainA
Resolution3.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F141 Q255 H257 L267 E270 R273 R301 H369 Y370 R405
Catalytic site (residue number reindexed from 1) F141 Q255 H257 L267 E270 R273 R301 H369 Y370 R405
Enzyme Commision number 1.3.5.1: succinate dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000104 succinate dehydrogenase activity
GO:0000166 nucleotide binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0009061 anaerobic respiration
GO:0022900 electron transport chain
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5xmj, PDBe:5xmj, PDBj:5xmj
PDBsum5xmj
PubMed30297797
UniProtT2GB49

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