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5LL3

Structure of the Isoleucine 2-epimerase from Lactobacillus buchneri (PLP complex form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008483molecular_functiontransaminase activity
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
B0008483molecular_functiontransaminase activity
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
C0008483molecular_functiontransaminase activity
C0016853molecular_functionisomerase activity
C0030170molecular_functionpyridoxal phosphate binding
C0042802molecular_functionidentical protein binding
D0008483molecular_functiontransaminase activity
D0016853molecular_functionisomerase activity
D0030170molecular_functionpyridoxal phosphate binding
D0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue PLP A 1000
ChainResidue
ASER114
AASN253
ALYS280
AHOH1101
AHOH1110
AHOH1122
BPHE308
BTHR309
AGLY115
ASER116
AASN119
ATYR142
AHIS143
AGLU217
AASP250
AVAL252

site_idAC2
Number of Residues22
Detailsbinding site for Di-peptide PLP B 1000 and LYS B 280
ChainResidue
APHE308
ATHR309
AHOH1102
BALA54
BALA56
BSER114
BGLY115
BSER116
BASN119
BTYR142
BHIS143
BGLU217
BASP250
BVAL252
BASN253
BGLY279
BSER281
BLEU282
BGLY285
BHOH1101
BHOH1104
BHOH1116

site_idAC3
Number of Residues22
Detailsbinding site for Di-peptide PLP C 1000 and LYS C 280
ChainResidue
CALA54
CALA56
CSER114
CGLY115
CSER116
CTYR142
CHIS143
CGLU217
CASP250
CVAL252
CASN253
CGLY279
CSER281
CLEU282
CGLY285
CHOH1101
CHOH1103
CHOH1115
CHOH1206
DPHE308
DTHR309
DHOH1106

site_idAC4
Number of Residues22
Detailsbinding site for Di-peptide PLP D 1000 and LYS D 280
ChainResidue
CPHE308
CTHR309
DALA54
DALA56
DSER114
DGLY115
DSER116
DASN119
DTYR142
DHIS143
DGLU217
DASP250
DVAL252
DASN253
DGLY279
DSER281
DLEU282
DGLY285
DHOH1101
DHOH1102
DHOH1105
DHOH1125

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues39
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FAiDEVnq.GLgRtGkmwaiqqfkdiep...DLMsvGKslaSG
ChainResidueDetails
APHE247-GLY285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22256","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P22256","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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