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6IX3

The structure of LepI complex with SAM

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0044550biological_processsecondary metabolite biosynthetic process
A0046983molecular_functionprotein dimerization activity
B0008168molecular_functionmethyltransferase activity
B0008171molecular_functionO-methyltransferase activity
B0016740molecular_functiontransferase activity
B0032259biological_processmethylation
B0044550biological_processsecondary metabolite biosynthetic process
B0046983molecular_functionprotein dimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue SAM A 401
ChainResidue
ALEU193
AHIS277
AARG291
ALEU292
AHOH516
AHOH556
AHOH609
AHOH645
AGLY227
AGLY229
AASP252
ALEU253
AVAL256
AHIS274
AASN275
APHE276

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 402
ChainResidue
ATYR241
APRO242
AASN243
AGLN244
BPRO279

site_idAC3
Number of Residues17
Detailsbinding site for residue SAM B 401
ChainResidue
BPHE189
BLEU193
BGLY227
BGLY229
BASP252
BVAL256
BHIS274
BASN275
BPHE276
BHIS277
BARG291
BLEU292
BHOH559
BHOH567
BHOH570
BHOH631
BHOH648

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
APHE135
BPHE135

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O04385
ChainResidueDetails
AGLY227
AASN275
AARG291
BGLY227
BASN275
BARG291

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01020
ChainResidueDetails
AASP252
BASP252

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PDB entries from 2025-06-18

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