Structure of PDB 3o0n Chain A

Receptor sequence
>3o0nA (length=607) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKDLDGNYLETKWEDVARRVAR
VVATAELLNPSYKKNEKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLG
VKHDLLWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAV
KEYALITKVGGGVGSNFSELRPKGSFVAGTHGKASGPVSFMHVFNSAISV
VALMGILNINHPDIEEFIDAKKVLNFFNLSVGFPMDKKEILKLYEEDGEL
ELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNKYYPLYPHR
KINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQELVQIAVRF
LDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIPYNSQEARD
FAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFVPFAMGMSN
YDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEPNFLLAYTL
LYVNQVLREKLNPEILKRIEKELIEKGSLKDIPDVPEKIKKVFVVALDID
PMDHLLMQDAFQRYVDNNISKTINMPQSATVDDVLNVYLEALRTNVRGIT
VYRDGSL
3D structure
PDB3o0n Structural Basis for Adenosylcobalamin Activation in AdoCbl-Dependent Ribonucleotide Reductases.
ChainA
Resolution1.95 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 N306 C308 E310 C319 T600 V601
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 R171 A178 G179 A184 S185 F190 D141 S142 I143 R171 A178 G179 A184 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3o0n, PDBe:3o0n, PDBj:3o0n
PDBsum3o0n
PubMed20672854
UniProtO33839

[Back to BioLiP]