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2WGD

Crystal structure of KasA of Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006633biological_processfatty acid biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0019367biological_processfatty acid elongation, saturated fatty acid
A0030497biological_processfatty acid elongation
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1416
ChainResidue
APHE275
AALA282
AASP283
AHOH2178
AHOH2179

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1417
ChainResidue
AHOH2180
AHOH2181
AALA18
AVAL19
AGLU30
AARG363

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1418
ChainResidue
AGLU199
AGLY200
APRO201
AILE202
AGLU203
APRO206
APHE239
ASER346
AHOH2182

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA A 1419
ChainResidue
AMET213
AILE317
AHOH2138
AHOH2183

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1420
ChainResidue
AASN309
AALA310
AGLU354
AASN399
AASN400

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1421
ChainResidue
AARG289
ATHR292
AVAL328

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1kas
ChainResidueDetails
AHIS345
AHIS311
APHE404
ACYS171

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1kas
ChainResidueDetails
AHIS345
AHIS311
APHE404
ALYS340
ACYS171
APHE402

222036

PDB entries from 2024-07-03

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