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1CSM

THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004106molecular_functionchorismate mutase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006571biological_processtyrosine biosynthetic process
A0008152biological_processmetabolic process
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009094biological_processL-phenylalanine biosynthetic process
A0016853molecular_functionisomerase activity
A0046417biological_processchorismate metabolic process
A0072545molecular_functionL-tyrosine binding
A0120284molecular_functiontryptophan binding
B0003824molecular_functioncatalytic activity
B0004106molecular_functionchorismate mutase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006571biological_processtyrosine biosynthetic process
B0008152biological_processmetabolic process
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009094biological_processL-phenylalanine biosynthetic process
B0016853molecular_functionisomerase activity
B0046417biological_processchorismate metabolic process
B0072545molecular_functionL-tyrosine binding
B0120284molecular_functiontryptophan binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRP B 501
ChainResidue
AILE74
AARG76
AGLU82
BASN138
BASN139
BPHE140
BGLY141
BSER142
BHOH516

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TRP A 502
ChainResidue
AASN138
AASN139
APHE140
AGLY141
ASER142
ATHR145
AHOH527
AHOH536
AHOH563
AHOH574
BILE74
BARG76
BGLU82
BHOH521

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:8622937, ECO:0007744|PDB:2CSM
ChainResidueDetails
AARG75
BGLY141
BSER142
BTHR145
AARG76
AASN139
AGLY141
ASER142
ATHR145
BARG75
BARG76
BASN139

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:7971967, ECO:0007744|PDB:1CSM
ChainResidueDetails
AASN138
BASN138

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 81
ChainResidueDetails
AARG16hydrogen bond donor, transition state stabiliser
AARG157hydrogen bond donor, transition state stabiliser
ALYS168hydrogen bond donor, transition state stabiliser
AASN194transition state stabiliser
AGLU198hydrogen bond acceptor, transition state stabiliser
ATHR242transition state stabiliser
AGLU246hydrogen bond donor, transition state stabiliser

site_idMCSA2
Number of Residues7
DetailsM-CSA 81
ChainResidueDetails
BARG16hydrogen bond donor, transition state stabiliser
BARG157hydrogen bond donor, transition state stabiliser
BLYS168hydrogen bond donor, transition state stabiliser
BASN194transition state stabiliser
BGLU198hydrogen bond acceptor, transition state stabiliser
BTHR242transition state stabiliser
BGLU246hydrogen bond donor, transition state stabiliser

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PDB entries from 2024-04-24

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