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2C43

STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE- PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008897molecular_functionholo-[acyl-carrier-protein] synthase activity
A0009258biological_process10-formyltetrahydrofolate catabolic process
A0015939biological_processpantothenate metabolic process
A0016740molecular_functiontransferase activity
A0019878biological_processlysine biosynthetic process via aminoadipic acid
A0046872molecular_functionmetal ion binding
A0051604biological_processprotein maturation
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A1317
ChainResidue
AASP139
AMET141
AGLU191
ACOA1316
AHOH2176

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A1318
ChainResidue
AGLN51
AARG74
AARG78

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE COA A1316
ChainResidue
AARG96
ALYS99
AGLY100
ALYS101
APRO102
AASN118
AILE119
ASER120
AHIS121
AASP139
ATRP187
AGLU191
AILE194
ALYS195
AGLY198
AGLY200
ALEU201
ALEU205
AMG1317
AHOH2036
AHOH2066
AHOH2102
AHOH2175
AHOH2176
AHOH2177
AHOH2178
AHOH2179
AHOH2180
AARG57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18022563, ECO:0007744|PDB:2C43, ECO:0007744|PDB:2CG5
ChainResidueDetails
AARG57
AARG96
AASN118

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18022563, ECO:0007744|PDB:2C43
ChainResidueDetails
AASP139
AGLU191

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER268

224201

PDB entries from 2024-08-28

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