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2QLT

Crystal structure of an isoform of DL-glycerol-3-phosphatase, Rhr2p, from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000121molecular_functionsn-glycerol 1-phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006114biological_processglycerol biosynthetic process
A0006970biological_processresponse to osmotic stress
A0016787molecular_functionhydrolase activity
A0043136molecular_functionsn-glycerol 3-phosphatase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG A 274
ChainResidue
ALEU227
ALYS228
ALYS230
ACYS232
AILE235
ACL279

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 275
ChainResidue
AHIS239
APHE38
AALA117
ACYS121

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 276
ChainResidue
AARG178
AALA211
AGLY212
ACYS213

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 277
ChainResidue
AHIS72
AHIS75
AHOH449

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 278
ChainResidue
AASP39
AASP41
AASP200
ASO4280
AHOH500
AHOH501

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 279
ChainResidue
ACYS232
AASP233
AILE234
AILE235
ATYR263
AHG274

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 280
ChainResidue
AASP39
AVAL40
AASP41
AGLY76
ATHR136
ASER137
AGLY138
ALYS168
ACA278
AHOH438
AHOH442

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 281
ChainResidue
AARG56
APHE65
AALA67
AGLU68
AHOH301
AHOH352
AHOH432
AHOH447

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 282
ChainResidue
ALYS60
ALYS209
AHOH460
AHOH512

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 283
ChainResidue
AALA52
AARG56
AHIS72
AGLN166
AHIS170
AHOH476

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 284
ChainResidue
AARG140
ALYS144
AARG154

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 285
ChainResidue
ALYS237
AASN238
AHOH387
AHOH444
AHOH487

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
ATHR136
ALYS168

249697

PDB entries from 2026-02-25

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