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1MDB

CRYSTAL STRUCTURE OF DhbE IN COMPLEX WITH DHB-ADENYLATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008668molecular_function(2,3-dihydroxybenzoyl)adenylate synthase activity
A0016874molecular_functionligase activity
A0019290biological_processsiderophore biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 999
ChainResidue
ALYS3
ALYS75
AARG77
AHOH643

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 997
ChainResidue
ATHR418
AARG419

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP A 600
ChainResidue
ALYS309
AVAL329
APHE330
AGLY331
AMET332
AALA333
ATHR411
AASP413
AVAL425
AARG428
ALYS519
ADBH601
AHOH699
AHOH736
AHOH836
AHIS234
AGLY307
AALA308

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DBH A 601
ChainResidue
AHIS234
AASN235
ATYR236
ASER240
AGLY307
AVAL329
AGLY331
AMET332
AALA333
AVAL337
ALYS519
AAMP600

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. LQLSGGSTGlSK
ChainResidueDetails
ALEU187-LYS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12221282
ChainResidueDetails
AGLY191
ASER240
AGLY307
AVAL329
AASP413
AARG428
ALYS519
AHIS234

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PDB entries from 2024-04-17

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