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4U04

Structure of a eukaryotic fic domain containing protein

Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue TAR A 501
ChainResidue
AGLU234
AHIS363
AASP367
AGLY368
AASN369
AGLY370
AARG371
AHOH643

site_idAC2
Number of Residues4
Detailsbinding site for residue PG4 A 502
ChainResidue
ALEU354
ATYR357
ALYS358
ATRP337

site_idAC3
Number of Residues2
Detailsbinding site for residue PG4 B 501
ChainResidue
BTRP337
BLYS358

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:22266942
ChainResidueDetails
AHIS363
BHIS363

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0U
ChainResidueDetails
AGLU234
BGLU234

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S, ECO:0007744|PDB:4U0U
ChainResidueDetails
AVAL316
ATYR399
AASN407
BVAL316
BTYR399
BASN407

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07
ChainResidueDetails
AASP367
BASP367

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for autoinhibition of adenylyltransferase activity => ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:25435325
ChainResidueDetails
AGLU234
BGLU234

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: O-AMP-threonine; by autocatalysis => ECO:0000305|PubMed:25601083
ChainResidueDetails
ATHR183
BTHR183

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25601083
ChainResidueDetails
AASN275
BASN275

225946

PDB entries from 2024-10-09

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