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3LOG

Crystal structure of MbtI from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0000287molecular_functionmagnesium ion binding
A0004106molecular_functionchorismate mutase activity
A0005886cellular_componentplasma membrane
A0008909molecular_functionisochorismate synthase activity
A0009058biological_processbiosynthetic process
A0009697biological_processsalicylic acid biosynthetic process
A0010106biological_processcellular response to iron ion starvation
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0016853molecular_functionisomerase activity
A0019540biological_processcatechol-containing siderophore biosynthetic process
A0043904molecular_functionisochorismate pyruvate lyase activity
A0046872molecular_functionmetal ion binding
A0052572biological_processresponse to host immune response
B0000162biological_processtryptophan biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004106molecular_functionchorismate mutase activity
B0005886cellular_componentplasma membrane
B0008909molecular_functionisochorismate synthase activity
B0009058biological_processbiosynthetic process
B0009697biological_processsalicylic acid biosynthetic process
B0010106biological_processcellular response to iron ion starvation
B0016829molecular_functionlyase activity
B0016833molecular_functionoxo-acid-lyase activity
B0016853molecular_functionisomerase activity
B0019540biological_processcatechol-containing siderophore biosynthetic process
B0043904molecular_functionisochorismate pyruvate lyase activity
B0046872molecular_functionmetal ion binding
B0052572biological_processresponse to host immune response
C0000162biological_processtryptophan biosynthetic process
C0000287molecular_functionmagnesium ion binding
C0004106molecular_functionchorismate mutase activity
C0005886cellular_componentplasma membrane
C0008909molecular_functionisochorismate synthase activity
C0009058biological_processbiosynthetic process
C0009697biological_processsalicylic acid biosynthetic process
C0010106biological_processcellular response to iron ion starvation
C0016829molecular_functionlyase activity
C0016833molecular_functionoxo-acid-lyase activity
C0016853molecular_functionisomerase activity
C0019540biological_processcatechol-containing siderophore biosynthetic process
C0043904molecular_functionisochorismate pyruvate lyase activity
C0046872molecular_functionmetal ion binding
C0052572biological_processresponse to host immune response
D0000162biological_processtryptophan biosynthetic process
D0000287molecular_functionmagnesium ion binding
D0004106molecular_functionchorismate mutase activity
D0005886cellular_componentplasma membrane
D0008909molecular_functionisochorismate synthase activity
D0009058biological_processbiosynthetic process
D0009697biological_processsalicylic acid biosynthetic process
D0010106biological_processcellular response to iron ion starvation
D0016829molecular_functionlyase activity
D0016833molecular_functionoxo-acid-lyase activity
D0016853molecular_functionisomerase activity
D0019540biological_processcatechol-containing siderophore biosynthetic process
D0043904molecular_functionisochorismate pyruvate lyase activity
D0046872molecular_functionmetal ion binding
D0052572biological_processresponse to host immune response
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SIN A 450
ChainResidue
ATYR385
ALEU404
AARG405
AALA418
AGLY419
ALYS438
AHOH468
AHOH604
AHOH627

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SIN A 451
ChainResidue
AARG382
AGLY383
ALEU384
ATYR385
ATYR408
ATRP415
AHOH529
AHOH996
AHOH1271

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 452
ChainResidue
AGLY270
AGLU294
AGLU297
AGLY421
AHOH517
AHOH546
AHOH1185
AHOH1443

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SIN B 450
ChainResidue
BTHR361
BTYR385
BARG405
BALA418
BGLY419
BLYS438
BCO3452
BHOH494
BHOH557
BHOH582

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA B 451
ChainResidue
BLYS293
BGLU297
BGLY421
BGLU431
BGLU434
BCO3452
BHOH648

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO3 B 452
ChainResidue
BGLY270
BTHR271
BGLU297
BGLY421
BGLU434
BLYS438
BSIN450
BNA451
BHOH558

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 453
ChainResidue
BVAL214
BPHE216
BALA217
BGLY412
BARG413
BTHR414
BHOH618

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SIN C 450
ChainResidue
CTHR361
CTYR385
CLEU404
CARG405
CALA418
CGLY419
CLYS438
CHOH1399
CHOH1490

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 451
ChainResidue
CVAL214
CPRO215
CPHE216
CALA217
CGLY412
CTHR414
CHOH538

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 452
ChainResidue
CARG80
CARG81
CHOH1533

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SIN D 450
ChainResidue
DTHR361
DTYR385
DLEU404
DARG405
DALA418
DGLY419
DLYS438
DHOH716
DHOH1558

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL D 451
ChainResidue
DARG382
DGLY383
DLEU384
DTYR385
DTYR408
DTRP415
DHOH503
DHOH1206
DHOH1394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9X9I8
ChainResidueDetails
AGLU252
BGLU252
CGLU252
DGLU252

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697
ChainResidueDetails
AGLY270
BGLY270
CGLY270
DGLY270

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20512795
ChainResidueDetails
AGLU297
AGLU431
AGLU434
BGLU297
BGLU431
BGLU434
CGLU297
CGLU431
CGLU434
DGLU297
DGLU431
DGLU434

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697
ChainResidueDetails
BTYR385
BARG405
BGLY419
BLYS438
CTYR385
CARG405
CGLY419
CLYS438
DTYR385
DARG405
DGLY419
DLYS438
ATYR385
AARG405
AGLY419
ALYS438

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl => ECO:0000269|PubMed:17240979
ChainResidueDetails
ALEU268
BLEU268
CLEU268
DLEU268

221051

PDB entries from 2024-06-12

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