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2YHK

D214A mutant of tyrosine phenol-lyase from Citrobacter freundii

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 K A 500
ChainResidue
AGLY52
AASN262
AHOH2082
AHOH2263
BGLU69
BHOH2246

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PG4 A 600
ChainResidue
AHOH2181
BGLN108
BLYS132
BASN133
BTYR285
ALYS132
AASN133
ATYR285

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 601
ChainResidue
ALEU109
AILE111
AHOH2384

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 603
ChainResidue
ALEU186
AARG381
ALEU400
ATHR402
AHOH2170

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 604
ChainResidue
ALYS226
ATYR312
AHOH2385

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PLP A 1257
ChainResidue
AGLN98
AGLY99
AARG100
APHE123
AASN185
ATHR216
AARG217
ASER254
ALYS257
AHOH2083
AHOH2149

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 500
ChainResidue
AGLU69
AHOH2103
AHOH2283
BGLY52
BASN262

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE P33 B 600
ChainResidue
ATYR3
ATYR324
ATYR414
AASP418
AHOH2357
BTYR3
BALA415
BASP418
BHOH2004

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 601
ChainResidue
BLEU109
BILE111
BLYS112

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PLP B 1257
ChainResidue
AHOH2108
BGLN98
BGLY99
BARG100
BPHE123
BASN185
BTHR216
BARG217
BSER254
BLYS257
BHOH2127

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
ATYR71proton acceptor, proton donor
APHE123steric role
ATHR124electrostatic stabiliser
AALA214electrostatic 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
BALA214electrostatic stabiliser
BLYS257covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BARG381electrostatic stabiliser
BPHE448electrostatic stabiliser, ground state destabiliser

219869

PDB entries from 2024-05-15

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