Structure of PDB 1xjf Chain B

Receptor sequence
>1xjfB (length=611) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKDLDGNYLETKWEDVARRVAR
VVATAELLNPSYKKNEKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLG
VKHDLLWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAV
KEYALITKVGGGVGSNFSELRPKGSFVAGTHGKASGPVSFMHVFNSAISV
VKQGRGALMGILNINHPDIEEFIDAKKVLNFFNLSVGFPMDKKEILKLYE
EDGELELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNKYYP
LYPHRKINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQELVQ
IAVRFLDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIPYNS
QEARDFAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFVPFA
MGMSNYDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEPNFL
LAYTRLYVNQVLREKLNPEILKRIEKELIEKGSLKDIPDVPEKIKKVFVV
ALDIDPMDHLLMQDAFQRYVDNNISKTINMPQSATVDDVLNVYLEALRTN
VRGITVYRDGS
3D structure
PDB1xjf Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase.
ChainB
Resolution2.4 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 N311 C313 E315 C324 T605 V606
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 DTP B K158 V201 K202 K158 V201 K202
BS02 DTP B D141 S142 I143 R171 V177 A178 G179 T180 S185 F190 D141 S142 I143 R171 V177 A178 G179 T180 S185 F190
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:1xjf, PDBe:1xjf, PDBj:1xjf
PDBsum1xjf
PubMed15475969
UniProtO33839

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