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6I7H

Crystal structure of dimeric FICD mutant K256S

Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 501
ChainResidue
AHOH601
AHOH606
AHOH641
AHOH700
AHOH734
AHOH740

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:22266942
ChainResidueDetails
AHIS363

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0U
ChainResidueDetails
AGLU234

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S, ECO:0007744|PDB:4U0U
ChainResidueDetails
AVAL316
ATYR399
AASN407

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07
ChainResidueDetails
AASP367

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for autoinhibition of adenylyltransferase activity => ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:25435325
ChainResidueDetails
AGLU234

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: O-AMP-threonine; by autocatalysis => ECO:0000305|PubMed:25601083
ChainResidueDetails
ATHR183

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25601083
ChainResidueDetails
AASN275

222415

PDB entries from 2024-07-10

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