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2YCN

Y71F mutant of tyrosine phenol-lyase from Citrobacter freundii in complex with quinonoid intermediate formed with 3-fluoro-L-tyrosine

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 K A 500
ChainResidue
AGLY52
AASN262
BGLU69
BHOH2102
BHOH2285

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE P61 A 600
ChainResidue
AARG100
AGLU103
APHE123
ATHR124
ATHR125
AASN185
AASP214
ATHR216
AARG217
ASER254
ALYS257
AMET379
AARG381
AARG404
APHE448
APHE449
AHOH2170
AHOH2328
BPHE71
APHE36
ATHR49
AGLN98
AGLY99

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 500
ChainResidue
AGLU69
AHOH2223
BGLY52
BASN262
BHOH2261

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE P61 B 600
ChainResidue
APHE71
BTHR49
BGLN98
BGLY99
BARG100
BGLU103
BPHE123
BTHR125
BASN185
BASP214
BTHR216
BARG217
BSER254
BLYS256
BLYS257
BARG381
BARG404
BHOH2085
BHOH2414
BHOH2415

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 A 1457
ChainResidue
AMET1
ATYR3
AALA5
ATYR324
ATYR414
BALA415
BASP418
BVAL419
BASP422
BHOH2374

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 1458
ChainResidue
AALA415
AHOH2330
BTYR3
BTYR324

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_idMCSA1
Number of Residues7
DetailsM-CSA 933
ChainResidueDetails
APHE71proton 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
BPHE71proton 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 2024-07-24

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