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6ABX

Crystal structure of citrate synthase (Msed_1522) from Metallosphaera sedula in complex with citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0036440molecular_functioncitrate synthase activity
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0006099biological_processtricarboxylic acid cycle
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0036440molecular_functioncitrate synthase activity
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue FLC A 401
ChainResidue
AHIS179
AARG332
AGOL403
AHOH505
AHOH553
AHOH639
BARG351
AASN182
AHIS214
AGLY215
AGLY216
AHIS253
AARG262
AASN305
AVAL306

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 402
ChainResidue
ALYS65
AALA69
APRO144
ALEU146
ASER147
AHOH507
AHOH520
AHOH606

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 403
ChainResidue
AGLY215
AGLY216
AGLY250
APHE251
AASN305
AASP307
AFLC401
AHOH553

site_idAC4
Number of Residues12
Detailsbinding site for residue FLC B 401
ChainResidue
AARG351
BHIS179
BASN182
BHIS214
BHIS253
BARG262
BASP307
BARG332
BHOH595
BHOH608
BHOH631
BHOH646

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL B 402
ChainResidue
BLYS65
BSER66
BPRO144
BLEU146
BSER147
BHOH593
BHOH605

Functional Information from PROSITE/UniProt
site_idPS00480
Number of Residues13
DetailsCITRATE_SYNTHASE Citrate synthase signature. GFGHrIy.KtmDPR
ChainResidueDetails
AGLY250-ARG262

239492

PDB entries from 2025-07-30

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