Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6AXE

Crystal structure of a malate synthase G from Mycobacterium marinum bound to acetyl CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004474molecular_functionmalate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0009436biological_processglyoxylate catabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004474molecular_functionmalate synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0009436biological_processglyoxylate catabolic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue ACO A 801
ChainResidue
AVAL118
AARG339
ALEU465
AMET519
ATRP545
APRO547
APRO549
ACYS623
ALYS625
AMET635
AASP637
AVAL119
AHOH907
AHOH955
AHOH984
AHOH1078
AHOH1156
AHOH1206
AHOH1210
AHOH1251
AHOH1313
AHOH1487
APRO120
AHOH1496
AHOH1543
AHOH1571
AARG125
APHE126
AASN129
AALA130
ASER275
AARG312

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 802
ChainResidue
AGLU438
AASP466
AHOH1088
AHOH1543
AHOH1571

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 803
ChainResidue
ALEU76
AASP77
APRO78
AILE585
AHOH1028

site_idAC4
Number of Residues24
Detailsbinding site for residue ACO B 801
ChainResidue
BVAL118
BVAL119
BARG125
BPHE126
BASN129
BTYR139
BASP140
BTYR143
BGLY144
BTYR160
BGLY165
BVAL168
BILE169
BILE249
BLYS305
BARG312
BPRO549
BTHR550
BMET635
BHOH943
BHOH1044
BHOH1086
BHOH1210
BHOH1496

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 802
ChainResidue
BPHE310
BARG312
BHOH1181
BHOH1371
BHOH1427

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 803
ChainResidue
BGLU438
BASP466
BHOH910
BHOH1141
BHOH1239
BHOH1503

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
AARG339
BARG339

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
AASP637
BASP637

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
AVAL118
BVAL118
BARG125
BSER275
BARG312
BARG339
BGLU438
BGLY463
BASP466
BPRO547
AARG125
ASER275
AARG312
AARG339
AGLU438
AGLY463
AASP466
APRO547

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00641
ChainResidueDetails
ACYS623
BCYS623

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon