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5JJQ

Crystal structure of IdnL1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016874molecular_functionligase activity
A0031177molecular_functionphosphopantetheine binding
A0043041biological_processamino acid activation for nonribosomal peptide biosynthetic process
A0044550biological_processsecondary metabolite biosynthetic process
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0016874molecular_functionligase activity
B0031177molecular_functionphosphopantetheine binding
B0043041biological_processamino acid activation for nonribosomal peptide biosynthetic process
B0044550biological_processsecondary metabolite biosynthetic process
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0016874molecular_functionligase activity
C0031177molecular_functionphosphopantetheine binding
C0043041biological_processamino acid activation for nonribosomal peptide biosynthetic process
C0044550biological_processsecondary metabolite biosynthetic process
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0016874molecular_functionligase activity
D0031177molecular_functionphosphopantetheine binding
D0043041biological_processamino acid activation for nonribosomal peptide biosynthetic process
D0044550biological_processsecondary metabolite biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 6L1 A 601
ChainResidue
AASP216
ATHR317
AVAL320
AASP408
AARG423
ALYS429
AARG434
ASER289
AGLY290
APRO292
AASN312
ACYS313
APHE314
AGLY315
ASER316

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 602
ChainResidue
AHIS342
AALA343
AMET349
AARG412

site_idAC3
Number of Residues18
Detailsbinding site for residue 6L1 B 601
ChainResidue
BASP216
BSER289
BGLY290
BGLU291
BPRO292
BASN312
BCYS313
BPHE314
BGLY315
BSER316
BTHR317
BVAL320
BASP408
BARG423
BLYS429
BARG434
BHOH730
BHOH731

site_idAC4
Number of Residues4
Detailsbinding site for residue CL B 602
ChainResidue
BHIS342
BALA343
BMET349
BARG412

site_idAC5
Number of Residues15
Detailsbinding site for residue 6L1 C 601
ChainResidue
CASP216
CSER289
CGLY290
CASN312
CCYS313
CPHE314
CGLY315
CSER316
CTHR317
CVAL320
CASP408
CARG423
CLYS429
CARG434
CHOH720

site_idAC6
Number of Residues3
Detailsbinding site for residue CL C 602
ChainResidue
CALA343
CMET349
CARG412

site_idAC7
Number of Residues15
Detailsbinding site for residue 6L1 D 601
ChainResidue
DASP216
DSER289
DGLY290
DASN312
DCYS313
DPHE314
DGLY315
DSER316
DTHR317
DVAL320
DASP408
DARG423
DLYS429
DARG434
DHOH721

site_idAC8
Number of Residues4
Detailsbinding site for residue CL D 602
ChainResidue
DHIS342
DALA343
DMET349
DARG412

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. MVFTSGSTGrPK
ChainResidueDetails
AMET168-LYS179

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PDB entries from 2026-01-21

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