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2ART

Crystal structure of lipoate-protein ligase A bound with lipoyl-AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009249biological_processprotein lipoylation
A0016874molecular_functionligase activity
A0016979molecular_functionlipoate-protein ligase activity
A0017118molecular_functionlipoyltransferase activity
A0031405molecular_functionlipoic acid binding
A0032991cellular_componentprotein-containing complex
A0036211biological_processprotein modification process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1301
ChainResidue
ATHR137
AASP138
AGLY148
AALA149
ALPA301
AAMP302

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LPA A 301
ChainResidue
AVAL79
AHIS81
ALYS145
AGLY148
AALA149
AHIS161
AALA163
AAMP302
AMG1301
AILE46
AARG72
AGLY77

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP A 302
ChainResidue
AGLY77
AVAL79
ATYR80
AASP85
APRO132
ALYS135
AASP138
ALYS145
AGLY148
AALA163
ALEU165
ALEU173
ALEU177
ALPA301
AMG1301
AHOH1308
AHOH1335
AHOH1377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16141198, ECO:0007744|PDB:2ARU
ChainResidueDetails
AARG72

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16141198, ECO:0007744|PDB:2ART, ECO:0007744|PDB:2ARU
ChainResidueDetails
AGLY77
ATYR80
AASP85
APRO132
ALYS135
ALYS145
AALA163

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16141198, ECO:0000269|PubMed:16384580, ECO:0007744|PDB:2ARS, ECO:0007744|PDB:2ART, ECO:0007744|PDB:2ARU
ChainResidueDetails
ATHR137
AASP138
AALA149

221716

PDB entries from 2024-06-26

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