Structure of PDB 3hnc Chain A

Receptor sequence
>3hncA (length=714) Species: 9606 (Homo sapiens) [Search protein sequence]
MFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAET
AATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHS
PMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKV
AERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRP
QLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIA
GTNGNSNGLVPMLRVYNNTARYVDQGAFAIYLEPWHLDIFEFLDLKKRDL
FFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQG
RVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNL
CTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLN
KIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLN
KQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDL
WDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRR
VLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQ
LYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGW
KQGLKTGMYYLRTR
3D structure
PDB3hnc Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.
ChainA
Resolution2.41 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) C205 N399 C401 E403 C416 Y709 Y710
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 TTP A D226 S227 I228 I231 R256 I262 A263 G264 N270 D213 S214 I215 I218 R243 I249 A250 G251 N257
BS02 TTP A K243 Y285 V286 Q288 K230 Y272 V273 Q275
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3hnc, PDBe:3hnc, PDBj:3hnc
PDBsum3hnc
PubMed21336276
UniProtP23921|RIR1_HUMAN Ribonucleoside-diphosphate reductase large subunit (Gene Name=RRM1)

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