Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3KDY

X-ray crystal structure of tyrosine aminomutase mutant construct

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009403biological_processtoxin biosynthetic process
A0016829molecular_functionlyase activity
A0016841molecular_functionammonia-lyase activity
A0016853molecular_functionisomerase activity
A0017000biological_processantibiotic biosynthetic process
A0050368molecular_functionL-tyrosine 2,3-aminomutase activity
A0052883molecular_functiontyrosine ammonia-lyase activity
B0003824molecular_functioncatalytic activity
B0009403biological_processtoxin biosynthetic process
B0016829molecular_functionlyase activity
B0016841molecular_functionammonia-lyase activity
B0016853molecular_functionisomerase activity
B0017000biological_processantibiotic biosynthetic process
B0050368molecular_functionL-tyrosine 2,3-aminomutase activity
B0052883molecular_functiontyrosine ammonia-lyase activity
Functional Information from PROSITE/UniProt
site_idPS00488
Number of Residues17
DetailsPAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GSLGASGDLaPLShvaS
ChainResidueDetails
AGLY148-LEU166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18078753","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20577998","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"2,3-didehydroalanine (Ser)","evidences":[{"source":"PubMed","id":"17516659","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsCross-link: {"description":"5-imidazolinone (Ala-Gly)","evidences":[{"source":"PubMed","id":"17516659","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 245
ChainResidueDetails
ATYR63hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLY70electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 245
ChainResidueDetails
BTYR63hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLY70electrostatic stabiliser, hydrogen bond donor

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon