Structure of PDB 2cvy Chain A

Receptor sequence
>2cvyA (length=640) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TKQFSKVVEDLYRYVNAATGKPAPMISDDVYNIVMENKDKLNSAIVYDRD
FQYSYFGFKTLERSYLLRINGQVAERPQHLIMRVALGIHGRDIEAALETY
NLMSLKYFTHASPTLFNAGTPKPQMSSCFLVAMKEDSIEGIYDTLKECAL
ISKTAGGIGLHIHNIRSTGSYIAGTNGTSNGLIPMIRVFNNTARYVAFAL
YLEPWHADIFDFIDIRKNHGKEEIRARDLFPALWIPDLFMKRVEENGTWT
LFSPTSAPGLSDCYGDEFEALYTRYEKEGRGKTIKAQKLWYSILEAQTET
GTPFVVYKDACNRKSNQKNLGVIKSSNLCCEIVEYSAPDETAVCNLASVA
LPAFIETSEDGKTSTYNFKKLHEIAKVVTRNLNRVIDRNYYPVEEARKSN
MRHRPIALGVQGLADTFMLLRLPFDSEEARLLNIQIFETIYHASMEASCE
LAQKDGPYETFQGSPASQGILQFDMWDQKPYGMWDWDTLRKDIMKHGVRN
SLTMAPMPTASTSQILGYNECFEPVTSNMYSFQVVNPYLLRDLVDLGIWD
EGMKQYLITQNGSIQGLPNVPQELKDLYKTVWEISQKTIINMAADRSVYI
DQSHSLNLFLRAPTMGKLTSMHFYGWKKGLKTGMYYLRTQ
3D structure
PDB2cvy Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation
ChainA
Resolution2.4 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) C218 N426 C428 E430 C443 Y741 Y742
Catalytic site (residue number reindexed from 1) C128 N327 C329 E331 C344 Y635 Y636
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 peptide A E343 Q386 Q692 K693 G722 T725 S726 M727 F729 Y730 E244 Q287 Q586 K587 G616 T619 S620 M621 F623 Y624
BS02 TTP A D226 S227 I228 I231 R256 I262 A263 D136 S137 I138 I141 R166 I172 A173
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005971 ribonucleoside-diphosphate reductase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2cvy, PDBe:2cvy, PDBj:2cvy
PDBsum2cvy
PubMed16537479
UniProtP21524|RIR1_YEAST Ribonucleoside-diphosphate reductase large chain 1 (Gene Name=RNR1)

[Back to BioLiP]