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6I7G

Crystal structure of dimeric wild type FICD complexed with ATP

Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ATP A 501
ChainResidue
AGLU234
AARG374
ATYR399
ATYR400
ALEU403
AASN407
AHOH601
AHOH602
AHOH605
AHOH614
AVAL316
AHIS319
AVAL360
AHIS363
AGLY368
AASN369
AGLY370
AARG371

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 502
ChainResidue
ATYR361
AALA406
A1PE503
AHOH619

site_idAC3
Number of Residues3
Detailsbinding site for residue 1PE A 503
ChainResidue
ALYS358
ATYR361
APEG502

site_idAC4
Number of Residues18
Detailsbinding site for residue ATP B 501
ChainResidue
BGLU234
BHIS319
BVAL360
BHIS363
BGLY368
BASN369
BGLY370
BARG371
BARG374
BTYR399
BTYR400
BLEU403
BASN407
BHOH602
BHOH605
BHOH610
BHOH618
BHOH636

site_idAC5
Number of Residues3
Detailsbinding site for residue PG4 B 502
ChainResidue
BLYS358
BGLY409
B1PE503

site_idAC6
Number of Residues4
Detailsbinding site for residue 1PE B 503
ChainResidue
BTRP337
BLYS358
BTYR361
BPG4502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues66
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues66
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues270
DetailsDomain: {"description":"Fido","evidences":[{"source":"PROSITE-ProRule","id":"PRU00791","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsMotif: {"description":"Inhibitory (S/T)XXXE(G/N) motif","evidences":[{"source":"PubMed","id":"22266942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"22266942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25435325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4U07","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4U0U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25435325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4U07","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4U0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4U0U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25435325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4U07","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Important for autoinhibition of adenylyltransferase activity","evidences":[{"source":"PubMed","id":"22266942","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25435325","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"O-AMP-threonine; by autocatalysis","evidences":[{"source":"PubMed","id":"25601083","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25601083","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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