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2TPL

TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION

Functional Information from GO Data
ChainGOidnamespacecontents
A0006520biological_processamino acid metabolic process
A0006570biological_processtyrosine metabolic process
A0009072biological_processaromatic amino acid metabolic process
A0016829molecular_functionlyase activity
A0016830molecular_functioncarbon-carbon lyase activity
A0050371molecular_functiontyrosine phenol-lyase activity
B0006520biological_processamino acid metabolic process
B0006570biological_processtyrosine metabolic process
B0009072biological_processaromatic amino acid metabolic process
B0016829molecular_functionlyase activity
B0016830molecular_functioncarbon-carbon lyase activity
B0050371molecular_functiontyrosine phenol-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CS A 500
ChainResidue
AASN262
BGLU69
BHOH636
BHOH666
AGLY52

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CS B 500
ChainResidue
AGLU69
AHOH515
AHOH571
BGLY52
BASN262

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HPP B 600
ChainResidue
ATYR71
BTHR49
BARG404
BHOH684

site_idCS
Number of Residues3
DetailsMONOVALENT CATION BINDING SITE.
ChainResidue
AGLU69
BGLY52
BASN262

site_idPLP
Number of Residues5
DetailsPLP AND SUBSTRATE BINDING SITE.
ChainResidue
ALLP257
AASP214
AASN185
BTYR71
BARG404

Functional Information from PROSITE/UniProt
site_idPS00853
Number of Residues19
DetailsBETA_ELIM_LYASE Beta-eliminating lyases pyridoxal-phosphate attachment site. YaDgctMSGKKDcLVnIGG
ChainResidueDetails
ATYR247-GLY265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALLP257
BLLP257

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 9174368, 10775663
ChainResidueDetails
ALLP257
ATYR71
AARG381
APHE123
AASP214

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 9174368, 10775663
ChainResidueDetails
BTYR71
BARG381
BPHE123
BASP214

site_idMCSA1
Number of Residues7
DetailsM-CSA 933
ChainResidueDetails
ATYR71proton acceptor, proton donor
APHE123steric role
ATHR124electrostatic stabiliser
AASP214electrostatic stabiliser
ALLP257covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
AARG381electrostatic stabiliser
APHE448electrostatic stabiliser, ground state destabiliser

site_idMCSA2
Number of Residues7
DetailsM-CSA 933
ChainResidueDetails
BTYR71proton acceptor, proton donor
BPHE123steric role
BTHR124electrostatic stabiliser
BASP214electrostatic stabiliser
BLLP257covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BARG381electrostatic stabiliser
BPHE448electrostatic stabiliser, ground state destabiliser

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PDB entries from 2024-07-10

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