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5KR6

Directed Evolution of Transaminases By Ancestral Reconstruction. Using Old Proteins for New Chemistries

Functional Information from GO Data
ChainGOidnamespacecontents
A0008483molecular_functiontransaminase activity
A0030170molecular_functionpyridoxal phosphate binding
B0008483molecular_functiontransaminase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue PLP A 501
ChainResidue
ASER119
ALYS288
AHOH614
AHOH621
AHOH626
AHOH631
BTHR325
AGLY120
ASER121
ATYR153
AHIS154
AGLU226
AASP259
AVAL261
AVAL262

site_idAC2
Number of Residues24
Detailsbinding site for Di-peptide PLP B 501 and LYS B 288
ChainResidue
ATHR325
ATYR326
BLEU58
BCYS60
BSER119
BGLY120
BSER121
BTYR153
BHIS154
BGLY155
BGLU226
BASP259
BVAL261
BVAL262
BALA287
BGLY289
BLEU290
BTHR291
BSER292
BALA293
BHOH632
BHOH633
BHOH638
BHOH651

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEVvc.GFgRtGsmfgshhygmkp....DLItvAKgltSA
ChainResidueDetails
ALEU256-ALA293

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PDB entries from 2024-06-12

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