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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
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
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
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0000269|PubMed:9416600
ChainResidueDetails
ASER146
BSER146

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: in other chain => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC
ChainResidueDetails
AARG21
AARG166
AALA177
AHIS207
BARG21
BARG166
BALA177
BHIS207

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS
ChainResidueDetails
AHIS51
AASP169
AALA263
BHIS51
BASP169
BALA263

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC
ChainResidueDetails
AARG126
BARG126

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PDB entries from 2024-05-01

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