Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6P9K

Crystal structure of Mycobacterium tuberculosis KasA in complex with O6G

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 NA A 501
ChainResidue
AASN309
AALA310
AGLU354
AASN399
AASN400

site_idAC2
Number of Residues5
Detailsbinding site for residue IPA A 502
ChainResidue
AHOH727
AVAL278
AILE317
ATYR391
APHE404

site_idAC3
Number of Residues3
Detailsbinding site for residue IPA A 503
ChainResidue
AGLY115
ALEU116
AMET146

site_idAC4
Number of Residues3
Detailsbinding site for residue IPA A 504
ChainResidue
AASP69
ATYR82
AHOH770

site_idAC5
Number of Residues5
Detailsbinding site for residue IPA A 505
ChainResidue
AARG78
AASP332
AASP381
ALEU382
AASP383

site_idAC6
Number of Residues5
Detailsbinding site for residue IPA A 506
ChainResidue
AALA282
AASP283
AASN324
AHOH697
AHOH772

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL A 507
ChainResidue
AALA18
AVAL19
AGLU30

site_idAC8
Number of Residues8
Detailsbinding site for residue O6G A 508
ChainResidue
AGLY117
AGLU120
AGLU199
AGLY200
APRO201
AGLU203
APRO206
AILE347

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

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon