Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3HNC

Crystal structure of human ribonucleotide reductase 1 bound to the effector TTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000731biological_processDNA synthesis involved in DNA repair
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005635cellular_componentnuclear envelope
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0006206biological_processpyrimidine nucleobase metabolic process
A0006264biological_processmitochondrial DNA replication
A0006281biological_processDNA repair
A0008584biological_processmale gonad development
A0009185biological_processribonucleoside diphosphate metabolic process
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0009265biological_process2'-deoxyribonucleotide biosynthetic process
A0010212biological_processresponse to ionizing radiation
A0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
A0016491molecular_functionoxidoreductase activity
A0017076molecular_functionpurine nucleotide binding
A0021846biological_processcell proliferation in forebrain
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0043025cellular_componentneuronal cell body
A0051290biological_processprotein heterotetramerization
A0060041biological_processretina development in camera-type eye
A0061731molecular_functionribonucleoside-diphosphate reductase activity
A0070318biological_processpositive regulation of G0 to G1 transition
A0097718molecular_functiondisordered domain specific binding
A1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
B0000731biological_processDNA synthesis involved in DNA repair
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005635cellular_componentnuclear envelope
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0006206biological_processpyrimidine nucleobase metabolic process
B0006264biological_processmitochondrial DNA replication
B0006281biological_processDNA repair
B0008584biological_processmale gonad development
B0009185biological_processribonucleoside diphosphate metabolic process
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0009265biological_process2'-deoxyribonucleotide biosynthetic process
B0010212biological_processresponse to ionizing radiation
B0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
B0016491molecular_functionoxidoreductase activity
B0017076molecular_functionpurine nucleotide binding
B0021846biological_processcell proliferation in forebrain
B0042802molecular_functionidentical protein binding
B0042995cellular_componentcell projection
B0043025cellular_componentneuronal cell body
B0051290biological_processprotein heterotetramerization
B0060041biological_processretina development in camera-type eye
B0061731molecular_functionribonucleoside-diphosphate reductase activity
B0070318biological_processpositive regulation of G0 to G1 transition
B0097718molecular_functiondisordered domain specific binding
B1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 801
ChainResidue
ATTP802
AHOH921

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE TTP A 802
ChainResidue
AGLY264
ASER269
AASN270
AHOH793
AMG801
AHOH921
BLYS243
BTYR285
BVAL286
BASP287
BGLN288
BGLY289
AASP226
ASER227
AILE228
AILE231
AARG256
AILE262
AALA263

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 804
ChainResidue
AILE136
ATYR137
AASP138
AHOH982
BLYS382

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 805
ChainResidue
ASER687
AGLN688
ALYS689

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 809
ChainResidue
AALA201
ASER202
ATHR604
ASER606
ATHR607
AHOH826
AHOH860
AHOH892
AHOH919

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 801
ChainResidue
BTTP802
BHOH919

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE TTP B 802
ChainResidue
ALYS243
ATYR285
AVAL286
AASP287
AGLN288
BASP226
BSER227
BILE228
BILE231
BILE255
BARG256
BILE262
BALA263
BGLY264
BSER269
BASN270
BHOH793
BMG801
BHOH805
BHOH919

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 803
ChainResidue
BSER687
BGLN688
BLYS689
BHOH873
BHOH968
BHOH969

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 806
ChainResidue
BLYS5
BARG6
BTHR53
BHOH970

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 807
ChainResidue
BSER202
BPRO603
BTHR604
BALA605
BSER606
BTHR607
BHOH956

Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WkvLkekiakyGIRNsllIApmP
ChainResidueDetails
ATRP581-PRO603

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASN427
AGLU431
BASN427
BGLU431

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000250
ChainResidueDetails
ACYS429
BCYS429

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0007744|PDB:3HNE
ChainResidueDetails
ALYS5
BGLU11
BTHR53
BASP57
BASP226
BLYS243
BARG256
BALA263
AGLU11
ATHR53
AASP57
AASP226
ALYS243
AARG256
AALA263
BLYS5

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0007744|PDB:3HND
ChainResidueDetails
ASER202
BTHR604
ASER217
AASN427
AGLU431
ATHR604
BSER202
BSER217
BASN427
BGLU431

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Important for hydrogen atom transfer => ECO:0000250
ChainResidueDetails
ACYS218
ACYS444
BCYS218
BCYS444

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Important for electron transfer => ECO:0000250
ChainResidueDetails
ATYR737
ATYR738
BTYR737
BTYR738

site_idSWS_FT_FI7
Number of Residues4
DetailsSITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250
ChainResidueDetails
ACYS787
ACYS790
BCYS787
BCYS790

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS17
ALYS376
BLYS17
BLYS376

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR751
BTHR751

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon