Structure of PDB 1xjm Chain A

Receptor sequence
>1xjmA (length=622) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKDLDGNYLETKWEDVARRVAR
VVATAELLNPSYKKNEKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLG
VKHDLLWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAV
KEYALITKVGGGVGSNFSELRPKGSFVAGTHGKASGPVSFMHVFNSAISV
VKQALMGILNINHPDIEEFIDAKKEAVLNFFNLSVGFPMDKKEILKLYEE
DGELELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNKYYPL
YPHRKINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQELVQI
AVRFLDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIPYNSQ
EARDFAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFVPFAM
GMSNYDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEPNFLL
AYTRFVTKEDGTKEPLLYVNQVLREKLNPEILKRIEKELIEKGSLKDIPD
VPEKIKKVFVVALDIDPMDHLLMQDAFQRYVDNNISKTINMPQSATVDDV
LNVYLEALRTNVRGITVRDGSL
3D structure
PDB1xjm Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase.
ChainA
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 N310 C312 E314 C323 T616 V617
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 A D141 S142 I143 I146 R171 V177 A178 G179 A184 S185 F190 D141 S142 I143 I146 R171 V177 A178 G179 A184 S185 F190
BS02 TTP A R26 S91 E324 P490 T491 G492 S493 I494 R26 S91 E314 P480 T481 G482 S483 I484
BS03 TTP A K158 V201 K158 V201
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:1xjm, PDBe:1xjm, PDBj:1xjm
PDBsum1xjm
PubMed15475969
UniProtO33839

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