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6ZA6

M. tuberculosis salicylate synthase MbtI in complex with Ba2+

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 Residues6
Detailsbinding site for residue GOL A 501
ChainResidue
AVAL214
APHE216
AALA217
AGLY412
ATHR414
AHOH662

site_idAC2
Number of Residues9
Detailsbinding site for residue PO4 A 502
ChainResidue
AGLY421
AGLU434
ALYS438
AHOH699
AHOH731
AHOH870
AGLY270
ATHR271
AALA420

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 503
ChainResidue
AARG405
AGLY419
ALYS438
AHOH624

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL B 501
ChainResidue
BVAL214
BPRO215
BPHE216
BGLY412
BTHR414
BHOH670

site_idAC5
Number of Residues7
Detailsbinding site for residue BA B 502
ChainResidue
BGLU297
BGLY421
BGLU431
BGLU434
BPO4503
BHOH605
BHOH659

site_idAC6
Number of Residues12
Detailsbinding site for residue PO4 B 503
ChainResidue
BLYS205
BGLY270
BTHR271
BGLU297
BGLY421
BGLU434
BLYS438
BBA502
BHOH605
BHOH617
BHOH631
BHOH658

site_idAC7
Number of Residues5
Detailsbinding site for residue CL B 504
ChainResidue
BARG405
BGLY419
BLYS438
BHOH660
BHOH723

site_idAC8
Number of Residues1
Detailsbinding site for residue CL B 505
ChainResidue
BARG189

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL C 501
ChainResidue
CVAL214
CPHE216
CALA217
CGLY412
CTHR414
CHOH614

site_idAD1
Number of Residues9
Detailsbinding site for residue PO4 C 502
ChainResidue
CGLY270
CTHR271
CGLY421
CGLU434
CLYS438
CHOH602
CHOH607
CHOH624
CHOH713

site_idAD2
Number of Residues4
Detailsbinding site for residue CL C 503
ChainResidue
CTYR385
CALA418
CGLY419
CHOH750

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL D 501
ChainResidue
DVAL214
DPHE216
DALA217
DGLY412
DTHR414
DHOH672

site_idAD4
Number of Residues7
Detailsbinding site for residue BA D 502
ChainResidue
DGLU297
DGLY421
DGLU431
DGLU434
DPO4503
DHOH628
DHOH797

site_idAD5
Number of Residues12
Detailsbinding site for residue PO4 D 503
ChainResidue
DLYS205
DGLY270
DTHR271
DGLU297
DGLY421
DGLU434
DLYS438
DBA502
DHOH610
DHOH628
DHOH660
DHOH697

site_idAD6
Number of Residues4
Detailsbinding site for residue CL D 504
ChainResidue
DARG405
DGLY419
DLYS438
DHOH678

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
DGLU297
DGLU431
DGLU434
AGLU431
AGLU434
BGLU297
BGLU431
BGLU434
CGLU297
CGLU431
CGLU434

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

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

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PDB entries from 2024-11-06

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