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1K0E

THE CRYSTAL STRUCTURE OF AMINODEOXYCHORISMATE SYNTHASE FROM FORMATE GROWN CRYSTALS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0008152biological_processmetabolic process
A0008153biological_processpara-aminobenzoic acid biosynthetic process
A0009058biological_processbiosynthetic process
A0009356cellular_componentaminodeoxychorismate synthase complex
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016740molecular_functiontransferase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
A0046820molecular_function4-amino-4-deoxychorismate synthase activity
A0046982molecular_functionprotein heterodimerization activity
A0120284molecular_functiontryptophan binding
B0000162biological_processtryptophan biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0008152biological_processmetabolic process
B0008153biological_processpara-aminobenzoic acid biosynthetic process
B0009058biological_processbiosynthetic process
B0009356cellular_componentaminodeoxychorismate synthase complex
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016740molecular_functiontransferase activity
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
B0046820molecular_function4-amino-4-deoxychorismate synthase activity
B0046982molecular_functionprotein heterodimerization activity
B0120284molecular_functiontryptophan binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TRP A 601
ChainResidue
ALEU34
ASER242
AILE394
AHOH1049
AHIS35
ASER36
ATYR43
ASER44
AARG45
APHE46
APRO240
APHE241

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRP B 602
ChainResidue
BHIS35
BSER36
BTYR43
BSER44
BARG45
BPHE46
BPRO240
BPHE241
BSER242
BILE394
BHOH1144

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1701
ChainResidue
AARG410
AALA423
AGLY424
ALYS443

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU258
BGLU258

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: N6-(4-deoxychorismate)-lysine intermediate
ChainResidueDetails
ALYS274
BLYS274

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11841211
ChainResidueDetails
ASER36
BSER36

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ATYR43
APRO240
BTYR43
BPRO240

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 283
ChainResidueDetails
AGLU258activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS274activator, hydrogen bond donor, nucleofuge, nucleophile, polar/non-polar interaction

site_idMCSA2
Number of Residues2
DetailsM-CSA 283
ChainResidueDetails
BGLU258activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BLYS274activator, hydrogen bond donor, nucleofuge, nucleophile, polar/non-polar interaction

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PDB entries from 2024-03-27

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