Structure of PDB 1xje Chain A

Receptor sequence
>1xjeA (length=627) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKDLDGNYLETKWEDVARRVAR
VVATAELLNPSYKKNEKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLG
VKHDLLWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAV
KEYALITKVGGGVGSNFSELRPKGSFVAGTHGKASGPVSFMHVFNSAISV
VKQGSRRRGALMGILNINHPDIEEFIDAKKVLNFFNLSVGFPMDKKEILK
LYEEDGELELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNK
YYPLYPHRKINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQE
LVQIAVRFLDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIP
YNSQEARDFAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFV
PFAMGMSNYDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEP
NFLLAYTRFVTKEDGTKEPLLYVNQVLREKLNPEILKRIEKELIEKGSLK
DIPDVPEKIKKVFVVALDIDPMDHLLMQDAFQRYVDNNISKTINMPQSAT
VDDVLNVYLEALRTNVRGITVYRDGSL
3D structure
PDB1xje Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C134 N320 C322 E324 C333 T626 V627
Catalytic site (residue number reindexed from 1) C134 N314 C316 E318 C327 T620 V621
Enzyme Commision number 1.17.4.1: ribonucleoside-diphosphate reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005524 ATP binding
GO:0031419 cobalamin binding
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1xje, PDBe:1xje, PDBj:1xje
PDBsum1xje
PubMed15475969
UniProtO33839

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