Structure of PDB 3o0o Chain A

Receptor sequence
>3o0oA (length=612) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKLSDLISRWIDVEPSKNAQIILRDRYFMKDLDGNYLETKWEDVARRVAR
VVATAELLNPSKLDRIKEWEDIFFRVLKARLFIPNSPTLFNAGLGVKHDL
LWKPIDQMTLEDYEEIYRSRNHLHMLSACFVVPVGDSIEEIFEAVKEYAL
ITKVGGGVGSNFSELRPKGSFVAGTHGKASGPVSFMHVFNSAISVVKQGS
RRGALMGILNINHPDIEEFIDAKKVLNFFNLSVGFPMDKKEILKLYEEDG
ELELSHPRSTIRKKVKIRELFRKIATNAWKSGDPGLAFLGEMNKYYPLYP
HRKINSTNPCGEIGLSDYEACNLGSIDVAKFYNNGFVDLEALQELVQIAV
RFLDNVIDVNVFPIDKITKAVKESRRLGLGIMGFADLLYKLEIPYNSQEA
RDFAANLMAFIALHAHRTSYELGKEKGNFPLLEISRYRTEDNFVPFAMGM
SNYDDEIREVMKMTKEFRRNVALLTIAPTGSISNIADTSSGLEPNFLLAY
TRFPLLYVNQVLREKLNPEILKRIEKELIEKGSLKDIPDVPEKIKKVFVV
ALDIDPMDHLLMQDAFQRYVDNNISKTINMPQSATVDDVLNVYLEALRTN
VRGITVYRDGSL
3D structure
PDB3o0o Structural Basis for Adenosylcobalamin Activation in AdoCbl-Dependent Ribonucleotide Reductases.
ChainA
Resolution1.9 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) C129 N308 C310 E312 C321 T605 V606
Enzyme Commision number 1.17.4.1: ribonucleoside-diphosphate reductase.
Interaction with ligand
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:3o0o, PDBe:3o0o, PDBj:3o0o
PDBsum3o0o
PubMed20672854
UniProtO33839

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