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4L57

High resolutin structure of human cytosolic 5'(3')-deoxyribonucleotidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000255biological_processallantoin metabolic process
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
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
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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
AASP10
AASP12
AASP145
APO4202
AHOH311
AHOH320

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 A 202
ChainResidue
ATHR99
ASER100
ALYS112
ALYS134
AMG201
AGOL204
AHOH301
AHOH311
AHOH320
AHOH535
AASP10
AMET11
AASP12

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 203
ChainResidue
AASN186
AARG188
AGLU189
AHOH335
AHOH391
AHOH524
BHOH336
BHOH353

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
APHE18
AGLU19
APHE44
APO4202
AGOL207
AHOH320
AHOH326
AHOH500
AHOH510

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
APHE44
ASER100
AARG132
AHOH301
AHOH389
AHOH546

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 206
ChainResidue
AARG51
AASP59
AGLU117
AGLN118
AHOH318
AHOH332
AHOH520

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 207
ChainResidue
APHE18
APHE44
ALEU45
AALA46
AARG47
ATYR65
AGOL204
AHOH410
AHOH511

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 208
ChainResidue
AASN88
ALEU90
ATHR93
AHOH423
AHOH429

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 201
ChainResidue
BASP10
BASP12
BASP145
BPO4202
BHOH314
BHOH315

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 B 202
ChainResidue
BASP10
BMET11
BASP12
BTHR99
BSER100
BLYS112
BLYS134
BMG201
BGOL203
BHOH301
BHOH314
BHOH315
BHOH371

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 203
ChainResidue
BASP12
BPHE18
BPHE44
BLEU45
BPHE71
BLEU102
BPO4202
BHOH371
BHOH384
BHOH479

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 2024-08-07

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