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6L1L

Apo-BacF structure from Bacillus subtillis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0017000biological_processantibiotic biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0017000biological_processantibiotic biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue PLP A 401
ChainResidue
AGLY103
ALYS239
AARG247
BTYR66
ALYS104
ATYR128
AASN174
AASN178
AASP206
ATYR209
ASER236
ASER238

site_idAC2
Number of Residues12
Detailsbinding site for residue PLP B 401
ChainResidue
ATYR66
BGLY103
BLYS104
BTYR128
BASN174
BASN178
BASP206
BTYR209
BSER236
BSER238
BLYS239
BARG247

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKtfNMaGWRMA
ChainResidueDetails
ASER236-ALA249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q93ZN9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"Q93ZN9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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