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1OWB

Three Dimensional Structure Analysis Of The Variant R109L NADH Complex of Type II Citrate Synthase From E. Coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0004108molecular_functioncitrate (Si)-synthase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0034214biological_processprotein hexamerization
A0036440molecular_functioncitrate synthase activity
A0042802molecular_functionidentical protein binding
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
A0070404molecular_functionNADH binding
B0004108molecular_functioncitrate (Si)-synthase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0034214biological_processprotein hexamerization
B0036440molecular_functioncitrate synthase activity
B0042802molecular_functionidentical protein binding
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0070404molecular_functionNADH binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 2001
ChainResidue
AARG407
BHOH22
BHOH32
BASN1232
BALA1233
BARG1299
BARG1306

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AHOH3112
BLYS1055
AGLY414
ATYR415

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 2003
ChainResidue
BHOH22
BHOH59
BHIS1229
BASN1232
BLEU1259
BARG1299
BHIS1305
BARG1314
BARG1387

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 2004
ChainResidue
AASN232
AALA233
AARG299
AARG306
AHOH3010
AHOH3064
BILE1405
BARG1407

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2005
ChainResidue
ALYS55
AHOH3070
AHOH3129
BTHR1413
BGLY1414

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2006
ChainResidue
AHIS229
AASN232
AARG299
AHIS305
AARG314
AARG387
AHOH3010
AHOH3046
AHOH3103

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAD A 3000
ChainResidue
ATHR106
ATHR108
ALEU109
AHIS110
ATHR111
AMET112
AHIS114
ATYR145
AASP147
AILE159
APHE162
AARG163
ALYS167
AGLN182
AASN189

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAD B 3001
ChainResidue
BHOH265
BHOH339
BHOH481
BTHR1106
BTHR1108
BLEU1109
BHIS1110
BTHR1111
BMET1112
BHIS1114
BTYR1145
BPHE1162
BARG1163
BLYS1167
BGLN1182
BASN1189
BCYS1206

Functional Information from PROSITE/UniProt
site_idPS00480
Number of Residues13
DetailsCITRATE_SYNTHASE Citrate synthase signature. GFGHrVy.KnyDPR
ChainResidueDetails
AGLY302-ARG314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10117
ChainResidueDetails
AHIS305
AASP362
BHIS1305
BASP1362

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS282
BLYS1282

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
AHIS264
AASP362
AHIS305

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
BASP1362
BHIS1305
BHIS1264

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
AHIS264
AASP362
ASER234
AHIS305

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
BASP1362
BHIS1305
BHIS1264
BSER1234

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