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6DDO

Crystal structure of the single mutant (D52N) of the full-length NT5C2 in the basal state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000255biological_processallantoin metabolic process
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006204biological_processIMP catabolic process
A0008253molecular_function5'-nucleotidase activity
A0009117biological_processnucleotide metabolic process
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0046037biological_processGMP metabolic process
A0046040biological_processIMP metabolic process
A0046054biological_processdGMP metabolic process
A0046085biological_processadenosine metabolic process
A0046872molecular_functionmetal ion binding
A0050146molecular_functionnucleoside phosphotransferase activity
A0050483molecular_functionIMP 5'-nucleotidase activity
A0050484molecular_functionGMP 5'-nucleotidase activity
A0050689biological_processnegative regulation of defense response to virus by host
A0061630molecular_functionubiquitin protein ligase activity
A0070936biological_processprotein K48-linked ubiquitination
A0106411molecular_functionXMP 5'-nucleosidase activity
B0000255biological_processallantoin metabolic process
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006204biological_processIMP catabolic process
B0008253molecular_function5'-nucleotidase activity
B0009117biological_processnucleotide metabolic process
B0016740molecular_functiontransferase activity
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
B0046037biological_processGMP metabolic process
B0046040biological_processIMP metabolic process
B0046054biological_processdGMP metabolic process
B0046085biological_processadenosine metabolic process
B0046872molecular_functionmetal ion binding
B0050146molecular_functionnucleoside phosphotransferase activity
B0050483molecular_functionIMP 5'-nucleotidase activity
B0050484molecular_functionGMP 5'-nucleotidase activity
B0050689biological_processnegative regulation of defense response to virus by host
B0061630molecular_functionubiquitin protein ligase activity
B0070936biological_processprotein K48-linked ubiquitination
B0106411molecular_functionXMP 5'-nucleosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PO4 A 601
ChainResidue
AARG34
AVAL35
AVAL37
ATYR471
ATYR475
APHE477
AHOH722
AHOH778

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 A 602
ChainResidue
AMET53
AASP54
ATHR249
AASN250
ASER251
ALYS292
AASN52

site_idAC3
Number of Residues7
Detailsbinding site for residue PO4 B 601
ChainResidue
BARG34
BVAL35
BVAL37
BTYR471
BTYR475
BPHE477
BHOH739

site_idAC4
Number of Residues7
Detailsbinding site for residue PO4 B 602
ChainResidue
BASN52
BMET53
BASP54
BTHR249
BASN250
BSER251
BLYS292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:21396942
ChainResidueDetails
AASN52
BASN52

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21396942
ChainResidueDetails
AASP54
BASP54

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2J2C, ECO:0007744|PDB:2JC9, ECO:0007744|PDB:2JCM, ECO:0007744|PDB:2XCV, ECO:0007744|PDB:2XCW, ECO:0007744|PDB:2XJB, ECO:0007744|PDB:2XJC, ECO:0007744|PDB:2XJD, ECO:0007744|PDB:2XJE
ChainResidueDetails
AASN52
AASP54
BASN52
BASP54

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJB
ChainResidueDetails
AARG144
AARG456
BARG144
BARG456

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJC
ChainResidueDetails
AASN154
ALYS362
AGLN453
ATYR457
BASN154
BLYS362
BGLN453
BTYR457

site_idSWS_FT_FI6
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XCV, ECO:0007744|PDB:2XCW
ChainResidueDetails
AARG202
BLYS215
BTHR249
BASN250
BSER251
BLYS292
AASP206
ALYS215
ATHR249
AASN250
ASER251
ALYS292
BARG202
BASP206

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2J2C, ECO:0007744|PDB:2JC9, ECO:0007744|PDB:2JCM
ChainResidueDetails
AASP351
BASP351

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0007744|PDB:2JC9
ChainResidueDetails
AMET436
BMET436

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER418
ASER511
BSER418
BSER511

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER502
BSER502

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3V1L4
ChainResidueDetails
ASER527
BSER527

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PDB entries from 2024-11-06

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