Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2I7D

Structure of Human cytosolic deoxyribonucleotidase in complex with deoxyuridine, AlF4 and Mg2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006204biological_processIMP catabolic process
A0006249biological_processdCMP catabolic process
A0008252molecular_functionnucleotidase activity
A0008253molecular_function5'-nucleotidase activity
A0008254molecular_function3'-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
A0046038biological_processGMP catabolic process
A0046045biological_processTMP catabolic process
A0046050biological_processUMP catabolic process
A0046055biological_processdGMP catabolic process
A0046059biological_processdAMP catabolic process
A0046074biological_processdTMP catabolic process
A0046079biological_processdUMP catabolic process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0000166molecular_functionnucleotide binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006204biological_processIMP catabolic process
B0006249biological_processdCMP catabolic process
B0008252molecular_functionnucleotidase activity
B0008253molecular_function5'-nucleotidase activity
B0008254molecular_function3'-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
B0046038biological_processGMP catabolic process
B0046045biological_processTMP catabolic process
B0046050biological_processUMP catabolic process
B0046055biological_processdGMP catabolic process
B0046059biological_processdAMP catabolic process
B0046074biological_processdTMP catabolic process
B0046079biological_processdUMP catabolic process
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 728
ChainResidue
AASP10
AASP12
AASP145
AALF400
AHOH729
AHOH731

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 729
ChainResidue
BALF401
BHOH730
BHOH733
BASP10
BASP12
BASP145

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ALF A 400
ChainResidue
AASP10
AMET11
AASP12
ATHR99
ASER100
ALYS112
ALYS134
ADUR300
AMG728
AHOH729
AHOH731

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ALF B 401
ChainResidue
BASP10
BMET11
BASP12
BTHR99
BSER100
BLYS112
BLYS134
BDUR301
BMG729
BHOH730
BHOH733

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DUR A 300
ChainResidue
AASP12
APHE18
APHE44
ALEU45
AALA46
ASER100
APRO101
ALEU102
AALF400
AHOH731
AHOH759
AHOH782
AHOH821
AHOH859

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DUR B 301
ChainResidue
BASP12
BPHE18
BPHE44
BLEU45
BALA46
BSER100
BPRO101
BLEU102
BALF401
BHOH733
BHOH737
BHOH771
BHOH821
BHOH878

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q91
ChainResidueDetails
AASP10
AASP12

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q91
ChainResidueDetails
BASP10
BASP12

249524

PDB entries from 2026-02-18

PDB statisticsPDBj update infoContact PDBjnumon