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6J24

Crystal structure of a SAM-dependent methyltransferase LepI in complex with its substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0032259biological_processmethylation
A0044550biological_processsecondary metabolite biosynthetic process
B0008168molecular_functionmethyltransferase activity
B0008171molecular_functionO-methyltransferase activity
B0032259biological_processmethylation
B0044550biological_processsecondary metabolite biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue BYO B 401
ChainResidue
BHIS133
BLEU138
BARG295
BASP296
BTHR338
BCYS341
BALA345

site_idAC2
Number of Residues14
Detailsbinding site for residue SAM B 402
ChainResidue
BASP252
BLEU253
BVAL256
BHIS274
BASN275
BPHE276
BHIS277
BARG291
BLEU292
BILE293
BHOH532
BHOH541
BGLY227
BGLY229

site_idAC3
Number of Residues7
Detailsbinding site for residue BYO A 401
ChainResidue
AGLY130
AHIS133
ALEU138
APHE189
AALA345
BMET45
BSER48

site_idAC4
Number of Residues13
Detailsbinding site for residue SAM A 402
ChainResidue
AGLY227
AGLY229
AASP252
ALEU253
AVAL256
AHIS274
AASN275
APHE276
AHIS277
AARG291
ALEU292
AHOH508
AHOH529

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

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

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

222624

PDB entries from 2024-07-17

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