Structure of PDB 2xav Chain C

Receptor sequence
>2xavC (length=728) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGI
KTSDIHETIIKAAADLISRDAPDYQYLAARLAIFHLRKKAYGQFEPPALY
DHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEG
KYLVQNRVTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTF
KISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINATSSAIVKYVSQRAG
IGINAGRIRALGSPFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMW
HLEVESLLVLKNNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDITLFSPS
DVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFSLMMQERAST
GRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVNDENGEI
ALCTLSAFNLGAINNLDELEELAILAVRALDALLDYQDYPIPAAKRGAMG
RRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELA
KEQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALRESIKTH
GLRNSTLSALMPSETSSQISNATNGIEPPRGYVSIKASKDGILRQVVPDY
EHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSRFPSGKV
PMQQLLKDLLTAYKFGVKTLFYQNTRDG
3D structure
PDB2xav Site-Specific Incorporation of 3-Nitrotyrosine as a Probe of Pk(A) Perturbation of Redox-Active Tyrosines in Ribonucleotide Reductase.
ChainC
Resolution2.8 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) C225 N437 C439 E441 C462 F730 Y731
Catalytic site (residue number reindexed from 1) C222 N428 C430 E432 C453 F721 Y722
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 C L348 K708 V709 P710 M711 Q712 L719 K723 L339 K699 V700 P701 M702 Q703 L710 K714
BS02 peptide C E111 L120 E108 L117
Gene Ontology
Molecular Function
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
GO:0044183 protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0009185 ribonucleoside diphosphate metabolic process
GO:0009263 deoxyribonucleotide biosynthetic process
GO:0009265 2'-deoxyribonucleotide biosynthetic process
GO:0015949 nucleobase-containing small molecule interconversion
Cellular Component
GO:0005829 cytosol
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:2xav, PDBe:2xav, PDBj:2xav
PDBsum2xav
PubMed20518462
UniProtP00452|RIR1_ECOLI Ribonucleoside-diphosphate reductase 1 subunit alpha (Gene Name=nrdA)

[Back to BioLiP]