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6CTS

PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL 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
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE CIC A 700
ChainResidue
AARG46
AVAL315
AGLY317
ATYR318
AGLY319
AHIS320
AALA321
AARG329
AALA366
AALA367
AALA368
AARG164
AASN373
AARG401
AARG421
AHOH539
AHOH547
AHOH584
AHOH603
AHIS238
AASN242
ALEU273
AHIS274
AALA277
ALEU309
AVAL314

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 Residues3
DetailsACT_SITE:
ChainResidueDetails
AHIS274
AHIS320
AASP375

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 78
ChainResidueDetails
ASER244electrostatic stabiliser, hydrogen bond donor
AHIS274electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AHIS320electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AARG329electrostatic stabiliser
AASP375hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-04-17

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