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5CSC

STRUCTURE OF AN OPEN FORM OF CHICKEN HEART CITRATE SYNTHASE AT 2.8 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004108molecular_functionobsolete citrate (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_functionobsolete citrate (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 PROSITE/UniProt
site_idPS00480
Number of Residues13
DetailsCITRATE_SYNTHASE Citrate synthase signature. GYGHaVl.RktDPR
ChainResidueDetails
BGLY317-ARG329
AGLY317-ARG329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"O75390","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"description":"in chain B","evidences":[{"source":"UniProtKB","id":"O75390","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

site_idMCSA1
Number of Residues5
DetailsM-CSA 78
ChainResidueDetails
BSER244electrostatic stabiliser, hydrogen bond donor
BHIS274electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BHIS320electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BARG329electrostatic stabiliser
BASP375hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

239803

PDB entries from 2025-08-06

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