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3HND

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000731biological_processDNA synthesis involved in DNA repair
A0003824molecular_functioncatalytic activity
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
A0034451cellular_componentcentriolar satellite
A0036064cellular_componentciliary basal body
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
B0000166molecular_functionnucleotide binding
B0000731biological_processDNA synthesis involved in DNA repair
B0003824molecular_functioncatalytic activity
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
B0034451cellular_componentcentriolar satellite
B0036064cellular_componentciliary basal body
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 Residues1
DetailsBINDING SITE FOR RESIDUE MG A 801
ChainResidue
ATTP802

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE TTP A 802
ChainResidue
AGLY264
ASER269
AASN270
AMG801
AHOH910
BLYS243
BTYR285
BVAL286
BASP287
BGLN288
AASP226
BGLY289
ASER227
AILE228
AGLU229
AILE255
AARG256
AILE262
AALA263

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GDP A 803
ChainResidue
ASER202
ASER217
ACYS218
AALA245
AGLY246
AGLY247
AGLY295
AASN427
ALEU428
ACYS429
AGLU431
APRO603
ATHR604
AALA605
ASER606
ATHR607

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 805
ChainResidue
AILE136
ATYR137
AASP138
BLYS382

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 806
ChainResidue
AASN614
AGLU615
ATHR621

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 807
ChainResidue
ASER687
AGLN688
ALYS689

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 801
ChainResidue
BTTP802

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE TTP B 802
ChainResidue
ALYS243
ATYR285
AVAL286
AASP287
AGLN288
AGLY289
BASP226
BSER227
BILE228
BILE255
BARG256
BILE262
BALA263
BGLY264
BSER269
BASN270
BMG801

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GDP B 803
ChainResidue
BALA201
BSER202
BSER217
BCYS218
BALA245
BGLY246
BGLY247
BARG293
BASN427
BLEU428
BCYS429
BGLU431
BPRO603
BTHR604
BALA605
BSER606
BTHR607

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 804
ChainResidue
BSER687
BGLN688
BLYS689

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

237992

PDB entries from 2025-06-25

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