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2CSC

Structure of ternary complexes of CITRATE SYNTHASE WITH D-AND L-MALATE: mechanistic implications

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 Residues25
DetailsBINDING SITE FOR RESIDUE CMC A 700
ChainResidue
AARG46
ATYR318
AGLY319
AHIS320
AALA321
AALA366
AALA367
AALA368
AASN373
AVAL374
AASP375
AARG164
APHE397
AHOH539
AHOH547
AHOH585
AHOH603
AMLT702
ALEU273
AHIS274
AGLY275
ALEU309
AVAL314
AVAL315
AGLY317

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLT A 702
ChainResidue
AHIS238
AASN242
AHIS274
AHIS320
AARG329
AARG401
AARG421
AHOH584
AHOH586
ACMC700

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

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

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aj8
ChainResidueDetails
AASP375
AHIS320
AHIS274
ASER244

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PDB entries from 2024-05-01

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