Structure of PDB 3hnd Chain B

Receptor sequence

>3hndB (length=735) Species: 9606 (Homo sapiens) [Search protein sequence]

HVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYVTT
VELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYN
YINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLER
SYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASP
TLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVS
CIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEP
WHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCP
NECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTP
YMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNM
YVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGI
GVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPY
ETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMP
TASTAQILGNNESIEPYTSNIYTRREFQIVNPHLLKDLTERGLWHEEMKN
QIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQS
LNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTR

3D structure

PDB

3hnd Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.

Chain

Resolution

3.21 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	C218 N427 C429 E431 C444 Y737 Y738
Catalytic site (residue number reindexed from 1)	C215 N424 C426 E428 C441 Y730 Y731
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	TTP	B	K243 Y285 V286 Q288	K240 Y282 V283 Q285
BS02	TTP	B	D226 S227 I228 R256 I262 A263 G264 S269 N270	D223 S224 I225 R253 I259 A260 G261 S266 N267
BS03	GDP	B	A201 S202 S217 C218 A245 G247 R293 N427 L428 C429 E431 P603 T604 A605 S606 T607	A198 S199 S214 C215 A242 G244 R290 N424 L425 C426 E428 P600 T601 A602 S603 T604

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:0017076	purine nucleotide binding
GO:0042802	identical protein binding
GO:0061731	ribonucleoside-diphosphate reductase activity
GO:0097718	disordered domain specific binding

	Biological Process
GO:0000731	DNA synthesis involved in DNA repair
GO:0006206	pyrimidine nucleobase metabolic process
GO:0006264	mitochondrial DNA replication
GO:0006281	DNA repair
GO:0008584	male gonad development
GO:0009185	ribonucleoside diphosphate metabolic process
GO:0009263	deoxyribonucleotide biosynthetic process
GO:0009265	2'-deoxyribonucleotide biosynthetic process
GO:0010212	response to ionizing radiation
GO:0010971	positive regulation of G2/M transition of mitotic cell cycle
GO:0021846	cell proliferation in forebrain
GO:0051290	protein heterotetramerization
GO:0060041	retina development in camera-type eye
GO:0070318	positive regulation of G0 to G1 transition
GO:1900087	positive regulation of G1/S transition of mitotic cell cycle

	Cellular Component
GO:0005635	nuclear envelope
GO:0005737	cytoplasm
GO:0005739	mitochondrion
GO:0005829	cytosol
GO:0005971	ribonucleoside-diphosphate reductase complex
GO:0042995	cell projection
GO:0043025	neuronal cell body

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:3hnd, PDBe:3hnd, PDBj:3hnd
PDBsum	3hnd
PubMed	21336276
UniProt	P23921\|RIR1_HUMAN Ribonucleoside-diphosphate reductase large subunit (Gene Name=RRM1)

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