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4GFP

2.7 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in a second conformational state

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
A0005737cellular_componentcytoplasm
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 501
ChainResidue
AGLU14
AILE15
ACYS16

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 502
ChainResidue
AGLU14
ACYS255
AASP292

Functional Information from PROSITE/UniProt
site_idPS00104
Number of Residues15
DetailsEPSP_SYNTHASE_1 EPSP synthase signature 1. LDcGNSGTAIRlLsG
ChainResidueDetails
ALEU89-GLY103

site_idPS00885
Number of Residues19
DetailsEPSP_SYNTHASE_2 EPSP synthase signature 2. RvKETDRIaAMvdgLqkLG
ChainResidueDetails
AARG340-GLY358

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00210
ChainResidueDetails
AASP315

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:4EGR
ChainResidueDetails
ALYS21
AGLY95
ATHR96
AARG123
AGLN169
AARG346
AARG387

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.3, ECO:0000269|Ref.7, ECO:0007744|PDB:3SLH, ECO:0007744|PDB:4ZND
ChainResidueDetails
ASER22
AARG26
ASER167
AALA168
AASP315
ALYS342

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PDB entries from 2024-07-24

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