Structure of PDB 1xjm Chain B

Receptor sequence
>1xjmB (length=603) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKDLDGNYLETKWEDVARRVAR
VVATAELLNPSYKKNEKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLG
VKHDLLWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAV
KEYALITKVGGGVGSNFSELRPKGSFVAGTHGKASGPVSFMHVFNSAISV
VKALMGILNINHPDIEEFIDAKKVLNFFNLSVGFPMDKKEILKLYEEDGE
LELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNKYYPLYPH
RKINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQELVQIAVR
FLDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIPYNSQEAR
DFAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFVPFAMGMS
NYDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEPNFLLAYV
NQVLREKLNPEILKRIEKELIEKGSLKDIPDVPEKIKKVFVVALDIDPMD
HLLMQDAFQRYVDNNISKTINMPQSATVDDVLNVYLEALRTNVRGITVYR
DGS
3D structure
PDB1xjm 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 N307 C309 E311 C320 T597 V598
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 TTP B K158 V201 K158 V201
BS02 TTP B D141 S142 I143 R171 V177 A178 A184 F190 D141 S142 I143 R171 V177 A178 A184 F190
BS03 TTP B R26 S91 E324 P490 T491 G492 S493 I494 R26 S91 E311 P477 T478 G479 S480 I481
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

View graph for
Biological Process
External links
PDB RCSB:1xjm, PDBe:1xjm, PDBj:1xjm
PDBsum1xjm
PubMed15475969
UniProtO33839

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