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1TPL

THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 457
ChainResidue
AGLN98
AGLY99
AARG100
ASER254
ALYS256
ALYS257

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 457
ChainResidue
BGLN98
BGLY99
BARG100
BSER254
BLYS256
BLYS257
BHOH541

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 458
ChainResidue
APRO20
AARG21
AARG24

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 458
ChainResidue
BARG24

site_idPLA
Number of Residues7
Details
ChainResidue
ALYS257
AASP214
AASN185
ATYR71
AGLY99
AARG100
ASER254

site_idPLB
Number of Residues7
Details
ChainResidue
BASN185
BTYR71
BGLY99
BARG100
BSER254
BLYS257
BASP214

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
ALYS257
BLYS257

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
AASP214

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BASP214

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
AARG381
ATYR71
AASP214

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BARG381
BTYR71
BASP214

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
AASP214
ALYS256

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BASP214
BLYS256

site_idMCSA1
Number of Residues7
DetailsM-CSA 933
ChainResidueDetails
ATYR71proton acceptor, proton donor
APHE123steric role
ATHR124electrostatic stabiliser
AASP214electrostatic stabiliser
ALYS257covalently 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
BLYS257covalently 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 2024-10-30

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