Structure of PDB 1xjn Chain A

Receptor sequence
>1xjnA (length=618) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKLDGNYLETKWEDVARRVARV
VATAELLNPSYKKNEKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLGV
KHDLLWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAVK
EYALITKVGGGVGSNFSELRPKGSFVAGTGKASGPVSFMHVFNSAISVVK
QGGALMGILNINHPDIEEFIDAKKVLNFFNLSVGFPMDKKEILKLYEEDG
ELELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNKYYPLYP
HRKINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQELVQIAV
RFLDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIPYNSQEA
RDFAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFVPFAMGM
SNYDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEPNFLLAY
TRFVTKEDEPLLYVNQVLREKLNPEILKRIEKELIEKGSLKDIPDVPEKI
KKVFVVALDIDPMDHLLMQDAFQRYVDNNISKTINMPQSATVDDVLNVYL
EALRTNVRGITVYRDGSL
3D structure
PDB1xjn Structural Mechanism of Allosteric Substrate Specificity Regulation in a Ribonucleotide Reductase
ChainA
Resolution2.25 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) C133 N308 C310 E312 C321 T611 V612
Enzyme Commision number 1.17.4.1: ribonucleoside-diphosphate reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CDP A N90 S91 A133 A210 N320 C322 E324 P490 T491 G492 S493 I494 N89 S90 A132 A204 N308 C310 E312 P478 T479 G480 S481 I482
BS02 DTP A D141 S142 I143 I146 R171 V177 A178 F190 D140 S141 I142 I145 R170 V176 A177 F188
BS03 DTP A H127 K158 K202 H126 K157 K200
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:1xjn, PDBe:1xjn, PDBj:1xjn
PDBsum1xjn
PubMed15475969
UniProtO33839

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