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4X2A

Crystal structure of mouse glyoxalase I complexed with baicalein

Functional Information from GO Data
ChainGOidnamespacecontents
A0004462molecular_functionlactoylglutathione lyase activity
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006357biological_processregulation of transcription by RNA polymerase II
A0006749biological_processglutathione metabolic process
A0008270molecular_functionzinc ion binding
A0009438biological_processmethylglyoxal metabolic process
A0016829molecular_functionlyase activity
A0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
A0030316biological_processosteoclast differentiation
A0043066biological_processnegative regulation of apoptotic process
A0046872molecular_functionmetal ion binding
B0004462molecular_functionlactoylglutathione lyase activity
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006357biological_processregulation of transcription by RNA polymerase II
B0006749biological_processglutathione metabolic process
B0008270molecular_functionzinc ion binding
B0009438biological_processmethylglyoxal metabolic process
B0016829molecular_functionlyase activity
B0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
B0030316biological_processosteoclast differentiation
B0043066biological_processnegative regulation of apoptotic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 201
ChainResidue
AHIS127
AGLU173
A3WL203
BGLN34
BGLU100

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 202
ChainResidue
B3WL201
AGLN34
AGLU100
BHIS127
BGLU173

site_idAC3
Number of Residues13
Detailsbinding site for residue 3WL A 203
ChainResidue
AHIS127
AMET158
AGLU173
AILE180
AALA181
AZN201
AHOH389
BGLN34
BLEU61
BPHE63
BPHE68
BLEU70
BGLU100

site_idAC4
Number of Residues12
Detailsbinding site for residue 3WL B 201
ChainResidue
AGLN34
APHE63
APHE68
ALEU70
APHE93
AGLU100
AZN202
BHIS127
BMET158
BGLU173
BILE180
BILE183

Functional Information from PROSITE/UniProt
site_idPS00934
Number of Residues22
DetailsGLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrIkdpkKSldFYtrvLGL
ChainResidueDetails
AGLN34-LEU55

site_idPS00935
Number of Residues17
DetailsGLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD
ChainResidueDetails
AGLY118-ASP134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
AGLU173
BGLU173

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN
ChainResidueDetails
AGLN34
AGLU100
BGLN34
BGLU100

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN
ChainResidueDetails
AARG38
AASN104
BARG38
BASN104

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in other chain => ECO:0007744|PDB:4OPN
ChainResidueDetails
AARG123
ALYS157
BARG123
BLYS157

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: in other chain => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN
ChainResidueDetails
AHIS127
AGLU173
BHIS127
BGLU173

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q04760
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS88
BLYS88

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q04760
ChainResidueDetails
ATHR107
BTHR107

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000250
ChainResidueDetails
ACYS139
BCYS139

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS148
BLYS148

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数据于2024-03-27公开中

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