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1SAW

X-ray structure of homo sapiens protein FLJ36880

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006090biological_processpyruvate metabolic process
A0006107biological_processoxaloacetate metabolic process
A0008948molecular_functionoxaloacetate decarboxylase activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0018773molecular_functionacetylpyruvate hydrolase activity
A0034545molecular_functionfumarylpyruvate hydrolase activity
A0046872molecular_functionmetal ion binding
A0047621molecular_functionacylpyruvate hydrolase activity
A0050163molecular_functionoxaloacetate tautomerase activity
B0003824molecular_functioncatalytic activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006090biological_processpyruvate metabolic process
B0006107biological_processoxaloacetate metabolic process
B0008948molecular_functionoxaloacetate decarboxylase activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0018773molecular_functionacetylpyruvate hydrolase activity
B0034545molecular_functionfumarylpyruvate hydrolase activity
B0046872molecular_functionmetal ion binding
B0047621molecular_functionacylpyruvate hydrolase activity
B0050163molecular_functionoxaloacetate tautomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 225
ChainResidue
AGLU71
AGLU73
AASP102
ALYS123
AHOH320
AHOH353
AHOH358

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 225
ChainResidue
BGLU73
BASP102
BHOH246
BHOH272
BHOH273
BVAL23
BGLU71

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 226
ChainResidue
ALYS18
AASN19
AHOH312
BLYS18
BASN19
BHOH242

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
APRO118
ATRP119
AHOH352
BTRP119
BHOH226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:30348641, ECO:0007744|PDB:6FOG
ChainResidueDetails
AARG25
ALYS123
ATHR192
BARG25
BLYS123
BTHR192

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15551868, ECO:0000269|PubMed:30348641, ECO:0007744|PDB:1SAW, ECO:0007744|PDB:6FOG, ECO:0007744|PDB:6FOH
ChainResidueDetails
AGLU71
AGLU73
AASP102
BGLU71
BGLU73
BASP102

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6AYQ8
ChainResidueDetails
ASER40
BSER40

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8R0F8
ChainResidueDetails
ALYS113
BLYS113

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R0F8
ChainResidueDetails
ALYS115
BLYS115

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PDB entries from 2024-07-24

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