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6L1O

Product bound BacF structure from Bacillus subtillis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0017000biological_processantibiotic biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0017000biological_processantibiotic biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue TYR B 401
ChainResidue
ATYR66
BASN178
BTYR325
BARG367
BPMP402
APHE69
AVAL270
BPHE17
BGLN39
BGLY40
BLYS104
BTYR128
BGLU130

site_idAC2
Number of Residues14
Detailsbinding site for residue PMP B 402
ChainResidue
ATYR66
BGLY102
BGLY103
BLYS104
BTYR128
BASN174
BASN178
BASP206
BTYR209
BSER236
BSER238
BLYS239
BARG247
BTYR401

site_idAC3
Number of Residues13
Detailsbinding site for residue PLP A 401
ChainResidue
AGLY103
ALYS104
ATYR128
AASN174
AASN178
AASP206
AALA208
ATYR209
ASER236
ASER238
ALYS239
AARG247
BTYR66

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKtfNMaGWRMA
ChainResidueDetails
BSER236-ALA249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q93ZN9
ChainResidueDetails
AASN178
ATYR209
ASER236
AARG247
BGLY103
BTYR128
BASN178
BTYR209
BSER236
BARG247
AGLY103
ATYR128

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q93ZN9
ChainResidueDetails
BLYS239
ALYS239

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PDB entries from 2024-06-12

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