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2EZ2

Apo tyrosine phenol-lyase from Citrobacter freundii at pH 8.0

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 1500
ChainResidue
AGLY52
AASN262
AHOH1622
BGLU69
BHOH5602

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 1600
ChainResidue
ALYS256
ALYS257
AHOH1647
AHOH1811
BHOH5917
AGLN98
AGLY99
AARG100
ASER254

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 5500
ChainResidue
AGLU69
AHOH1618
BGLY52
BASN262
BHOH5613
BHOH5661

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 5600
ChainResidue
BGLN98
BGLY99
BARG100
BSER254
BLYS257
BHOH5638
BHOH5806
BHOH5926

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 Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
APHE123
AASP214

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BPHE123
BASP214

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
ATYR71
AARG381
APHE123
AASP214

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BTYR71
BARG381
BPHE123
BASP214

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
AASP214
ALYS256
ATYR128

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ax4
ChainResidueDetails
BASP214
BLYS256
BTYR128

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 2024-07-24

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