Structure of PDB 3hne Chain B

Receptor sequence
>3hneB (length=724) Species: 9606 (Homo sapiens) [Search protein sequence]
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSG
VTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMED
LYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKT
LERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTH
ASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGV
AVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGAFAIYLEPWH
LDIFEFLDLKKNRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDE
VWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSC
NRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTY
DFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADA
FILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPV
SKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQIL
GNNESIEPYTSNIYTFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQS
IPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYG
KLTSMHFYGWKQGLKTGMYYLRTR
3D structure
PDB3hne Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.
ChainB
Resolution3.11 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) C218 N427 C429 E431 C444 Y737 Y738
Catalytic site (residue number reindexed from 1) C218 N416 C418 E420 C433 Y719 Y720
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 B D226 S227 I228 R256 I262 A263 S269 D226 S227 I228 R256 I262 A263 S269
BS02 ATP B V3 K5 R6 E11 M14 K17 I18 T53 L56 V3 K5 R6 E11 M14 K17 I18 T53 L56
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:3hne, PDBe:3hne, PDBj:3hne
PDBsum3hne
PubMed21336276
UniProtP23921|RIR1_HUMAN Ribonucleoside-diphosphate reductase large subunit (Gene Name=RRM1)

[Back to BioLiP]