Structure of PDB 4erm Chain B

Receptor sequence
>4ermB (length=734) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGI
KTSDIHETIIKAAADLISRDAPDYQYLAARLAIFHLRKKAYGQFEPPALY
DHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEG
KYLVQNRVTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTF
KISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINATSSAIVKYVSQRAG
IGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAAT
LFYPMWHLEVESLLVLKNNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDI
TLFSPSDVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFSLMM
QERASTGRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVN
DENGEIALCTLSAFNLGAINNLDELEELAILAVRALDALLDYQDYPIPAA
KRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLK
ASNELAKEQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALR
ESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRGYVSIKASKDGILR
QVVPDYEHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSR
FPSGKVPMQQLLKDLLTAYKFGVKTLYYQNTRDG
3D structure
PDB4erm Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase.
ChainB
Resolution3.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C225 N437 C439 E441 C462 Y730 Y731
Catalytic site (residue number reindexed from 1) C222 N434 C436 E438 C459 Y727 Y728
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 DTP B V7 K9 R10 I17 N18 K21 T55 H59 F87 V4 K6 R7 I14 N15 K18 T52 H56 F84
BS02 DAT B T209 C225 C439 P621 S622 T624 S625 T206 C222 C436 P618 S619 T621 S622
BS03 DTP B D232 S233 L234 R262 I268 R269 H275 T276 D229 S230 L231 R259 I265 R266 H272 T273
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

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Molecular Function

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Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4erm, PDBe:4erm, PDBj:4erm
PDBsum4erm
PubMed22727814
UniProtP00452|RIR1_ECOLI Ribonucleoside-diphosphate reductase 1 subunit alpha (Gene Name=nrdA)

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