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3U6W

Truncated M. tuberculosis LeuA (1-425) complexed with KIV

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003852molecular_function2-isopropylmalate synthase activity
A0009098biological_processL-leucine biosynthetic process
A0019752biological_processcarboxylic acid metabolic process
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0003824molecular_functioncatalytic activity
B0003852molecular_function2-isopropylmalate synthase activity
B0009098biological_processL-leucine biosynthetic process
B0019752biological_processcarboxylic acid metabolic process
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 426
ChainResidue
AASP81
AHIS285
AHIS287
AKIV427

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 426
ChainResidue
BASP81
BHIS285
BHIS287
BKIV427

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE KIV A 427
ChainResidue
AASP81
ALEU143
ASER216
AGLU218
APRO252
ATHR254
AHIS285
AHIS287
AMN426
AARG80

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE KIV B 427
ChainResidue
BARG80
BASP81
BGLU218
BPRO252
BTHR254
BHIS285
BHIS287
BMN426

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 428
ChainResidue
APHE313
AASN315
AVAL352
AASN356
ALEU358
APRO359
BHIS361
BARG363

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 428
ChainResidue
AHIS361
AARG363
BPHE313
BASN315
BVAL352
BASN356
BLEU358
BPRO359
BVAL360
BHOH438

Functional Information from PROSITE/UniProt
site_idPS00815
Number of Residues17
DetailsAIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGnQalidPmsparK
ChainResidueDetails
ALEU79-LYS95

site_idPS00816
Number of Residues14
DetailsAIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. LslHpHNDrGtAvA
ChainResidueDetails
ALEU282-ALA295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15159544, ECO:0000269|PubMed:22352945, ECO:0000312|PDB:1SR9, ECO:0000312|PDB:3U6W
ChainResidueDetails
AARG80
ATHR254
BARG80
BTHR254

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:15159544, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:1SR9, ECO:0007744|PDB:3FIG, ECO:0007744|PDB:3HPS, ECO:0007744|PDB:3HPX, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1, ECO:0007744|PDB:3U6W
ChainResidueDetails
AASP81
AHIS285
AHIS287
BASP81
BHIS285
BHIS287

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1
ChainResidueDetails
AASN321
BASN321

222415

PDB entries from 2024-07-10

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