Structure of PDB 1xjj Chain B

Receptor sequence
>1xjjB (length=611) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKDLDGNYLETKWEDVARRVAR
VVATAELLNPSYKKNEKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLG
VKHDLLWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAV
KEYALITKVGGGVGSNFSELRPKGSFVAGTHGKASGPVSFMHVFNSAISV
VKQALMGILNINHPDIEEFIDAKKEAVLNFFNLSVGFPMDKKEILKLYEE
DGELELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNKYYPL
YPHRKINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQELVQI
AVRFLDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIPYNSQ
EARDFAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFVPFAM
GMSNYDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEPNFLL
AYTRFYVNQVLREKLNPEILKRIEKELIEKGSLKDIPDVPEKIKKVFVVA
LDIDPMDHLLMQDAFQRYVDNNISKTINMPQSATVDDVLNVYLEALRTNV
RGITVYRDGSL
3D structure
PDB1xjj Structural Mechanism of Allosteric Substrate Specificity Regulation in a Ribonucleotide Reductase
ChainB
Resolution1.86 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C134 N320 C322 E324 C333 T626 V627
Catalytic site (residue number reindexed from 1) C134 N310 C312 E314 C323 T604 V605
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 DGT B K158 V201 K158 V201
BS02 DGT B D141 S142 I143 R171 V177 S185 F190 D141 S142 I143 R171 V177 S185 F190
BS03 DGT B R26 S91 E324 P490 T491 G492 S493 R514 R26 S91 E314 P480 T481 G482 S483 R504
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1xjj, PDBe:1xjj, PDBj:1xjj
PDBsum1xjj
PubMed15475969
UniProtO33839

[Back to BioLiP]