Structure of PDB 1jnz Chain A

Receptor sequence
>1jnzA (length=642) Species: 224325 (Archaeoglobus fulgidus DSM 4304) [Search protein sequence]
VYYPKKYELYKADEVPTEVVETDILIIGGGFSGCGAAYEAAYWAKLGGLK
VTLVEKAAVERSGAVAQGLSAINTYIDLTGRSERQNTLEDYVRYVTLDMM
GLAREDLVADYARHVDGTVHLFEKWGLPIWKTPDGKYVREGQWQIMIHGE
SYKPIIAEAAKMAVGEENIYERVFIFELLKDNNDPNAVAGAVGFSVREPK
FYVFKAKAVILATGGATLLFRPRSTGEAAGRTWYAIFDTGSGYYMGLKAG
AMLTQFEHRFIPFRFKDGYGPVGAWFLFFKCKAKNAYGEEYIKTRAAELE
KYKPYGAAQPIPTPLRNHQVMLEIMDGNQPIYMHTEEALAELAGGDKKKL
KHIYEEAFEDFLDMTVSQALLWACQNIDPQEQPSEAAPAEPYIMGSHSGE
AGFWVCGPEDLMPEEYAKLFPLKYNRMTTVKGLFAIGDCAGANPHKFSSG
SFTEGRIAAKAAVRFILEQKPNPEIDDAVVEELKKKAYAPMERFMQYKDL
STADDVNPEYILPWQGLVRLQKIMDEYAAGIATIYKTNEKMLQRALELLA
FLKEDLEKLAARDLHELMRAWELVHRVWTAEAHVRHMLFRKETRWPGYYY
RTDYPELNDEEWKCFVCSKYDAEKDEWTFEKVPYVQVIEWSF
3D structure
PDB1jnz Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N74 E141 W234 R265 D361 H398 S449
Catalytic site (residue number reindexed from 1) N73 E140 W233 R264 D360 H397 S448
Enzyme Commision number 1.8.99.2: adenylyl-sulfate reductase.
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:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0009061 anaerobic respiration
Cellular Component
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jnz, PDBe:1jnz, PDBj:1jnz
PDBsum1jnz
PubMed11842205
UniProtO28603

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