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6I7J

Crystal structure of monomeric FICD mutant L258D

Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 A 501
ChainResidue
AARG217
AHIS363
AGLY368
AASN369
AGLY370
ASO4506
AHOH612

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 502
ChainResidue
ATYR400
AHOH622
ATHR239
ASER241

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 503
ChainResidue
AGLN112
AARG295
AGLY299
ATYR300
AHOH611
AHOH619

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 504
ChainResidue
ALYS203
ATYR386
AHOH607

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 505
ChainResidue
ASER241
AHIS245
ASER397
ATYR400
AHIS401

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 506
ChainResidue
AGLY370
ATYR399
ASO4501
APG4513
AHOH620

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 A 507
ChainResidue
AARG396
ATYR400
APG4513

site_idAC8
Number of Residues4
Detailsbinding site for residue 1PE A 508
ChainResidue
ATRP337
ATYR357
ALYS358
APG4512

site_idAC9
Number of Residues3
Detailsbinding site for residue 1PE A 509
ChainResidue
AMET219
ATYR224
AHOH633

site_idAD1
Number of Residues4
Detailsbinding site for residue 1PE A 510
ChainResidue
AILE320
AARG392
AASP427
APEG515

site_idAD2
Number of Residues2
Detailsbinding site for residue PG4 A 511
ChainResidue
ATYR161
AHOH642

site_idAD3
Number of Residues6
Detailsbinding site for residue PG4 A 512
ChainResidue
ATYR357
ALYS358
ATYR361
AALA406
AGLY409
A1PE508

site_idAD4
Number of Residues7
Detailsbinding site for residue PG4 A 513
ChainResidue
AHIS319
ATYR361
ATYR400
AGLU404
AASN407
ASO4506
ASO4507

site_idAD5
Number of Residues4
Detailsbinding site for residue PEG A 514
ChainResidue
AALA109
AGLN112
AMET135
ATYR300

site_idAD6
Number of Residues1
Detailsbinding site for residue PEG A 515
ChainResidue
A1PE510

site_idAD7
Number of Residues6
Detailsbinding site for residue PG4 A 516
ChainResidue
AVAL205
AMET206
AILE208
ALEU215
AMET219
ATYR386

site_idAD8
Number of Residues5
Detailsbinding site for residue PG4 A 517
ChainResidue
AGLY120
ALYS121
AARG122
AGLU123
ALYS124

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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