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4CTS

CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF A COMPLEX OF CITRATE SYNTHASE WITH OXALOACETATE AND S-ACETONYL-COENZYME A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004108molecular_functioncitrate (Si)-synthase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005975biological_processcarbohydrate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0006101biological_processcitrate metabolic process
A0016740molecular_functiontransferase activity
A0036440molecular_functioncitrate synthase activity
A0042802molecular_functionidentical protein binding
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0004108molecular_functioncitrate (Si)-synthase activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005975biological_processcarbohydrate metabolic process
B0006099biological_processtricarboxylic acid cycle
B0006101biological_processcitrate metabolic process
B0016740molecular_functiontransferase activity
B0036440molecular_functioncitrate synthase activity
B0042802molecular_functionidentical protein binding
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OAA A 438
ChainResidue
AHIS238
AASN242
AHIS274
AHIS320
AALA321
AARG329
AARG401
BARG421

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OAA B 438
ChainResidue
BHIS238
BASN242
BHIS274
BHIS320
BARG329
BARG401
AARG421

Functional Information from PROSITE/UniProt
site_idPS00480
Number of Residues13
DetailsCITRATE_SYNTHASE Citrate synthase signature. GYGHaVl.RktDPR
ChainResidueDetails
AGLY317-ARG329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE:
ChainResidueDetails
AHIS274
AHIS320
AASP375
BHIS274
BHIS320
BASP375

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q29RK1
ChainResidueDetails
ALYS49
BLYS49

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6
ChainResidueDetails
ALYS76
ALYS166
ALYS423
BLYS76
BLYS166
BLYS423

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CZU6
ChainResidueDetails
ASER199
BSER199

site_idSWS_FT_FI5
Number of Residues10
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6
ChainResidueDetails
ALYS294
BLYS432
ALYS300
ALYS348
ALYS366
ALYS432
BLYS294
BLYS300
BLYS348
BLYS366

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O75390
ChainResidueDetails
ALYS355
BLYS355

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:7093227
ChainResidueDetails
ALYS368
BLYS368

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
AASP375
AHIS274
AHIS320

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
BASP375
BHIS274
BHIS320

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
AASP375
AHIS320
AHIS274
ASER244

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
BASP375
BHIS320
BHIS274
BSER244

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PDB entries from 2024-07-17

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