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3A7R

Crystal structure of E. coli lipoate-protein ligase A in complex with lipoyl-AMP.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009249biological_processprotein lipoylation
A0016874molecular_functionligase activity
A0016979molecular_functionlipoate-protein ligase activity
A0017118molecular_functionlipoyltransferase activity
A0036211biological_processprotein modification process
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE LAQ A 401
ChainResidue
ATRP37
ALYS133
AGLY136
ATHR151
ALEU153
ALEU161
ALEU165
ASER179
AVAL180
AARG181
ASER182
AARG70
AVAL184
AHOH601
AHOH663
AHOH751
AHOH777
AHOH1036
AHOH1092
AMG1201
AGLY75
AALA76
AVAL77
APHE78
AHIS79
AASN83
AASN121

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG58
AARG59
AHOH960

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AASP305
AARG337
AHOH634
AHOH780
AHOH857
AHOH908
AHOH924
AHOH1052

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG277
AHOH818
AHOH957

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AHIS267
AGLN279
AHOH927
AHOH977
AHOH1021

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1201
ChainResidue
ALYS133
AVAL180
ASER182
ALAQ401
AHOH935

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues187
DetailsDomain: {"description":"BPL/LPL catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01067","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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