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5W2P

Crystal structure of Mycobacterium tuberculosis KasA in complex with 6U5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0019367biological_processfatty acid elongation, saturated fatty acid
A0030497biological_processfatty acid elongation
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 6U5 A 501
ChainResidue
AGLY117
AILE347
A6U5502
AGLU120
AGLU199
AGLY200
APRO201
AGLU203
APRO206
APHE239
AHIS345

site_idAC2
Number of Residues9
Detailsbinding site for residue 6U5 A 502
ChainResidue
AGLY115
ALEU116
AILE145
AMET146
AGLU199
ALEU205
APRO206
AILE347
A6U5501

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 503
ChainResidue
AALA18
AVAL19
AGLU30
ASER97

site_idAC4
Number of Residues5
Detailsbinding site for residue NA A 504
ChainResidue
AASN309
AALA310
AGLU354
AASN399
AASN400

site_idAC5
Number of Residues3
Detailsbinding site for residue IPA A 505
ChainResidue
AVAL278
AILE317
ATYR391

site_idAC6
Number of Residues4
Detailsbinding site for residue IPA A 506
ChainResidue
AARG79
ALEU156
AMET277
AHOH659

site_idAC7
Number of Residues2
Detailsbinding site for residue IPA A 507
ChainResidue
AASP28
AHOH617

site_idAC8
Number of Residues6
Detailsbinding site for residue TCE A 508
ChainResidue
ATRP95
APRO101
AGLU102
AVAL103
AGLN157
ALEU158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:19604480, ECO:0000305|PubMed:24108128, ECO:0000305|PubMed:24479625
ChainResidueDetails
ACYS171

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348
ChainResidueDetails
AHIS311
AHIS345

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:19604480, ECO:0000305|PubMed:24108128
ChainResidueDetails
AHIS311
AHIS345

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Interacts with the inhibitor thiolactomycin => ECO:0000269|PubMed:19604480, ECO:0000269|PubMed:24108128
ChainResidueDetails
ACYS171
AHIS311
AHIS345

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PDB entries from 2025-06-18

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