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3TO3

Crystal Structure of Petrobactin Biosynthesis Protein AsbB from Bacillus anthracis str. Sterne

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016874molecular_functionligase activity
A0016881molecular_functionacid-amino acid ligase activity
A0019290biological_processsiderophore biosynthetic process
B0005524molecular_functionATP binding
B0016874molecular_functionligase activity
B0016881molecular_functionacid-amino acid ligase activity
B0019290biological_processsiderophore biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 617
ChainResidue
AASP148
AASN152
AALA277
AGLN278
AARG285
AHOH718

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 618
ChainResidue
AHIS194
ALYS196
AASP262

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP B 617
ChainResidue
BGLY157
BHIS158
BSER280
BARG282
BLYS296
BARG308
BASN385
BTYR388
BHIS436
BGLY437
BGLN438
BASP456
BGLU459
BMG618
BHOH646
BHOH663
BHOH672
BHOH766
BHOH793

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 618
ChainResidue
BHIS436
BGLN438
BASN439
BASP456
BATP617

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 619
ChainResidue
BHIS194
BLYS196
BASP262
BGLY264

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 620
ChainResidue
BLYS528
BSER531

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 621
ChainResidue
BASN403

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:22408253, ECO:0007744|PDB:3TO3
ChainResidueDetails
ASER280
BGLU459
ALYS296
AARG308
ATYR388
AGLU459
BSER280
BLYS296
BARG308
BTYR388

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PDB entries from 2024-07-24

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