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3DX5

Crystal structure of the probable 3-DHS dehydratase AsbF involved in the petrobactin synthesis from Bacillus anthracis

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0046279biological_process3,4-dihydroxybenzoate biosynthetic process
A0046565molecular_function3-dehydroshikimate dehydratase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 287
ChainResidue
AGLU142
AASP172
AHIS198
ALYS200
AGLU253

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 288
ChainResidue
ALYS268
AHOH464
AGLN45
AGLU46
ATYR47
ALYS264

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DHB A 289
ChainResidue
AILE8
ATYR70
AARG102
AGLU142
AHIS144
AASP172
AHIS175
ALYS200
APHE211
ATYR217
AGLU253
APHE255
AHOH370

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 290
ChainResidue
ASER110
APHE113
AARG118
AHOH399
AHOH511
AHOH512
AHOH518

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 291
ChainResidue
ALEU54
ATRP95
ALYS97
AHOH357
AHOH364

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18955706","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18955706","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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