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6MQQ

Citrobacter freundii F448A mutant tyrosine phenol-lyase complexed with 4-hydroxypyridine and aminoacrylate from S-ethyl-L-cysteine

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 CQG A 601
ChainResidue
APHE123
ATHR124
AARG381
APHE449
BTYR71

site_idAC2
Number of Residues6
Detailsbinding site for residue K A 602
ChainResidue
BASN262
BHOH1775
AGLU69
AHOH750
AHOH761
BGLY52

site_idAC3
Number of Residues15
Detailsbinding site for residue 0JO A 603
ChainResidue
ATHR49
ASER51
AGLN98
AGLY99
AARG100
AGLU103
APHE123
AASN185
AASP214
AARG217
ASER254
ALYS257
AARG404
AHOH709
BTYR71

site_idAC4
Number of Residues6
Detailsbinding site for residue K A 604
ChainResidue
AGLY52
AASN262
AHOH756
AHOH774
BGLU69
BHOH1729

site_idAC5
Number of Residues5
Detailsbinding site for residue P33 B 1601
ChainResidue
ATYR3
ATYR414
BTYR3
BTYR324
BASP418

site_idAC6
Number of Residues2
Detailsbinding site for residue CQG B 1602
ChainResidue
BTYR3
BTYR324

site_idAC7
Number of Residues1
Detailsbinding site for residue CQG B 1603
ChainResidue
BARG323

site_idAC8
Number of Residues15
Detailsbinding site for residue 0JO B 1604
ChainResidue
ATYR71
BTHR49
BGLN98
BGLY99
BARG100
BGLU103
BPHE123
BASN185
BASP214
BTHR216
BARG217
BSER254
BLYS257
BARG404
BHOH1704

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
AASP214electrostatic stabiliser
ALYS257covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
AARG381electrostatic stabiliser
AALA448electrostatic 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
BALA448electrostatic stabiliser, ground state destabiliser

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PDB entries from 2024-07-24

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