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4F2V

Crystal Structure of de novo designed serine hydrolase, Northeast Structural Genomics Consortium (NESG) Target OR165

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0004799molecular_functionthymidylate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0006417biological_processregulation of translation
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0009314biological_processresponse to radiation
A0016740molecular_functiontransferase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0032259biological_processmethylation
A0042803molecular_functionprotein homodimerization activity
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0004799molecular_functionthymidylate synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006235biological_processdTTP biosynthetic process
B0006417biological_processregulation of translation
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0009314biological_processresponse to radiation
B0016740molecular_functiontransferase activity
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0032259biological_processmethylation
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LMU A 301
ChainResidue
AARG21
ASER173
APHE176
AGLY181
ALEU184
APEG302
AHOH415
AHOH428
AHOH461
BARG126
APHE62
ATRP83
ATRP98
AASN143
AALA144
ASER146
AARG166
ASER167

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 302
ChainResidue
APHE62
AHIS94
ATRP98
APRO145
ASER146
AHIS147
ALMU301

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LMU B 301
ChainResidue
AARG126
BPHE62
BILE79
BLEU80
BTRP83
BASN143
BALA144
BSER146
BARG166
BSER167
BSER173
BHOH443

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2223754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8973201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9416600","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"2223754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8973201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KCE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TSC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8312270","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TYS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"2223754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8973201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KCE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TSC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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