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5YRR

The crystal structure of Phosphopantetheine adenylyltransferase from Acinetobacter baumannii with Coenzyme A at 2.88 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0015937biological_processcoenzyme A biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue COA A 201
ChainResidue
AGLY10
ASER130
ATHR131
ALEU132
AARG134
AGLU135
AHOH301
AHOH312
ATHR11
ATHR16
AHIS19
AGLY73
ALEU75
AARG89
AARG92
AILE128

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 202
ChainResidue
ATHR131
AARG134

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 203
ChainResidue
AHIS41
AHIS42
ALYS43
AARG138
ALEU139

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 204
ChainResidue
APRO148
AGLN149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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