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4YIH

Crystal structure of human cytosolic 5'(3')-deoxyribonucleotidase in complex with the inhibitor PB-PVU

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000255biological_processallantoin metabolic process
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006204biological_processIMP catabolic process
A0006249biological_processdCMP catabolic process
A0008252molecular_functionnucleotidase activity
A0008253molecular_function5'-nucleotidase activity
A0009117biological_processnucleotide metabolic process
A0009223biological_processpyrimidine deoxyribonucleotide catabolic process
A0009264biological_processdeoxyribonucleotide catabolic process
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0019103molecular_functionpyrimidine nucleotide binding
A0042802molecular_functionidentical protein binding
A0043605biological_processamide catabolic process
A0046050biological_processUMP catabolic process
A0046055biological_processdGMP catabolic process
A0046074biological_processdTMP catabolic process
A0046079biological_processdUMP catabolic process
A0046872molecular_functionmetal ion binding
A0050483molecular_functionIMP 5'-nucleotidase activity
A0070062cellular_componentextracellular exosome
B0000166molecular_functionnucleotide binding
B0000255biological_processallantoin metabolic process
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006204biological_processIMP catabolic process
B0006249biological_processdCMP catabolic process
B0008252molecular_functionnucleotidase activity
B0008253molecular_function5'-nucleotidase activity
B0009117biological_processnucleotide metabolic process
B0009223biological_processpyrimidine deoxyribonucleotide catabolic process
B0009264biological_processdeoxyribonucleotide catabolic process
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0019103molecular_functionpyrimidine nucleotide binding
B0042802molecular_functionidentical protein binding
B0043605biological_processamide catabolic process
B0046050biological_processUMP catabolic process
B0046055biological_processdGMP catabolic process
B0046074biological_processdTMP catabolic process
B0046079biological_processdUMP catabolic process
B0046872molecular_functionmetal ion binding
B0050483molecular_functionIMP 5'-nucleotidase activity
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MG A 201
ChainResidue
AASP10
AASP12
AASP145
APO4202
A2O2203
AGOL204
AHOH358

site_idAC2
Number of Residues12
Detailsbinding site for residue PO4 A 202
ChainResidue
AASP12
ATHR99
ASER100
ALYS134
AMG201
A2O2203
AHOH358
AHOH313
AHOH351
AHOH377
AASP10
AMET11

site_idAC3
Number of Residues17
Detailsbinding site for residue 2O2 A 203
ChainResidue
AASP12
APHE18
APHE44
ALEU45
AALA46
AARG47
ATYR65
ASER100
ALEU102
ALEU103
AARG132
AMG201
APO4202
AGOL204
AHOH316
AHOH351
AHOH377

site_idAC4
Number of Residues11
Detailsbinding site for residue GOL A 204
ChainResidue
AASP12
AGLY13
APHE18
AGLU19
APHE44
AASP145
ACYS165
AHIS167
AMG201
A2O2203
AHOH310

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 201
ChainResidue
BASP10
BASP12
BASP145
BPO4202
B2O2203
BHOH344

site_idAC6
Number of Residues11
Detailsbinding site for residue PO4 B 202
ChainResidue
BASP10
BMET11
BASP12
BTHR99
BSER100
BLYS112
BLYS134
BMG201
B2O2203
BHOH344
BHOH317

site_idAC7
Number of Residues15
Detailsbinding site for residue 2O2 B 203
ChainResidue
BASP12
BPHE18
BPHE44
BLEU45
BALA46
BARG47
BTYR65
BLEU102
BLEU103
BARG132
BMG201
BPO4202
BHOH344
BHOH314
BHOH304

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
AASP10
BASP10

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AASP12
BASP12

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP10
BASP145
AASP12
APHE18
APHE44
AASP145
BASP10
BASP12
BPHE18
BPHE44

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATYR65
BTYR65

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ATHR99
ALYS134
BTHR99
BLYS134

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER182
BSER182

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PDB entries from 2024-09-11

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