Structure of PDB 5cnt Chain C

Receptor sequence

>5cntC (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

PDB

5cnt Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli.

Chain

Resolution

3.25 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)
BS01	UDP	C	T209 S224 C225 G253 Q294 R298 N437 L438 E441 L464 M620 P621 S622 T624 S625	T206 S221 C222 G250 Q291 R295 N434 L435 E438 L461 M617 P618 S619 T621 S622
BS02	DTP	C	V7 K9 R10 E15 N18 K21 V25 T55 H59 K91	V4 K6 R7 E12 N15 K18 V22 T52 H56 K88
BS03	DTP	C	K21 R24 W28 F97	K18 R21 W25 F94
BS04	DTP	C	D232 S233 L234 R262 I268 R269 H275 F281	D229 S230 L231 R259 I265 R266 H272 F278
BS05	DTP	C	S249 C292 S293	S246 C289 S290

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

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Biological Process

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Cellular Component

External links

PDB	RCSB:5cnt, PDBe:5cnt, PDBj:5cnt
PDBsum	5cnt
PubMed	26754917
UniProt	P00452\|RIR1_ECOLI Ribonucleoside-diphosphate reductase 1 subunit alpha (Gene Name=nrdA)

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