Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2V6K

Structure of Maleyl Pyruvate Isomerase, a bacterial glutathione-s- transferase in Zeta class, in complex with substrate analogue dicarboxyethyl glutathione

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0006559biological_processL-phenylalanine catabolic process
A0006749biological_processglutathione metabolic process
A0009056biological_processcatabolic process
A0009072biological_processaromatic amino acid metabolic process
A0016034molecular_functionmaleylacetoacetate isomerase activity
A0016853molecular_functionisomerase activity
A0050077molecular_functionmaleylpyruvate isomerase activity
A1901170biological_processnaphthalene catabolic process
B0003824molecular_functioncatalytic activity
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0006559biological_processL-phenylalanine catabolic process
B0006749biological_processglutathione metabolic process
B0009056biological_processcatabolic process
B0009072biological_processaromatic amino acid metabolic process
B0016034molecular_functionmaleylacetoacetate isomerase activity
B0016853molecular_functionisomerase activity
B0050077molecular_functionmaleylpyruvate isomerase activity
B1901170biological_processnaphthalene catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE TGG A1213
ChainResidue
ASER9
ASER65
APRO66
AHIS104
AASN108
AARG109
AARG110
AARG176
AHOH2010
AHOH2221
AHOH2360
AGLY10
AHOH2361
AHOH2362
AHOH2363
AHOH2364
AHOH2365
BCYS101
BASP102
BHOH2190
ATHR11
AARG14
ALEU33
AHIS38
ALEU51
AVAL52
AGLN64

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE TGG B1213
ChainResidue
ACYS101
AASP102
AHOH2216
BSER9
BGLY10
BTHR11
BARG14
BLEU33
BHIS38
BLEU51
BVAL52
BGLN64
BSER65
BPRO66
BHIS104
BASN108
BARG109
BARG110
BARG176
BHOH2011
BHOH2194
BHOH2196
BHOH2285
BHOH2343
BHOH2344
BHOH2345
BHOH2346
BHOH2347
BHOH2348

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A1214
ChainResidue
AARG175
AHOH2139
AHOH2141
AHOH2325

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B1214
ChainResidue
BARG175
BHOH2133
BHOH2284
BHOH2309

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A1215
ChainResidue
AARG109
AGLU113
AARG116
AHOH2366
AHOH2367

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B1215
ChainResidue
BARG109
BGLU113
BARG116
BHOH2349
BHOH2350

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:18824004
ChainResidueDetails
ASER9
BVAL52
BGLN64
BASP102
BASN108
BARG176
AHIS38
AVAL52
AGLN64
AASP102
AASN108
AARG176
BSER9
BHIS38

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
AASN5

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BASN5

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon