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6ZG1

SARM1 SAM1-2 domains

Functional Information from GO Data
ChainGOidnamespacecontents
A0003953molecular_functionNAD+ nucleosidase activity
A0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
A0035591molecular_functionsignaling adaptor activity
A0048678biological_processresponse to axon injury
B0003953molecular_functionNAD+ nucleosidase activity
B0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
B0035591molecular_functionsignaling adaptor activity
B0048678biological_processresponse to axon injury
C0003953molecular_functionNAD+ nucleosidase activity
C0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
C0035591molecular_functionsignaling adaptor activity
C0048678biological_processresponse to axon injury
D0003953molecular_functionNAD+ nucleosidase activity
D0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
D0035591molecular_functionsignaling adaptor activity
D0048678biological_processresponse to axon injury
E0003953molecular_functionNAD+ nucleosidase activity
E0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
E0035591molecular_functionsignaling adaptor activity
E0048678biological_processresponse to axon injury
F0003953molecular_functionNAD+ nucleosidase activity
F0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
F0035591molecular_functionsignaling adaptor activity
F0048678biological_processresponse to axon injury
G0003953molecular_functionNAD+ nucleosidase activity
G0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
G0035591molecular_functionsignaling adaptor activity
G0048678biological_processresponse to axon injury
H0003953molecular_functionNAD+ nucleosidase activity
H0034128biological_processnegative regulation of MyD88-independent toll-like receptor signaling pathway
H0035591molecular_functionsignaling adaptor activity
H0048678biological_processresponse to axon injury
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue EDO A 601
ChainResidue
ALYS428
ASER432
ALEU455

site_idAC2
Number of Residues2
Detailsbinding site for residue BME A 602
ChainResidue
ACYS482
ATYR503

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 603
ChainResidue
AGLY425
ALYS428
AARG465
BGLN437

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO B 601
ChainResidue
BLEU444
BGLY504

site_idAC5
Number of Residues8
Detailsbinding site for residue EDO B 602
ChainResidue
BALA477
BASN478
BTYR479
BSER480
BASP483
BASN486
BALA488
BARG499

site_idAC6
Number of Residues4
Detailsbinding site for residue PEG B 603
ChainResidue
BARG497
BGLN500
BHIS534
CSER507

site_idAC7
Number of Residues9
Detailsbinding site for residue PGE B 605
ChainResidue
BPRO402
BARG403
BPRO404
BTRP412
BGLU416
BTRP420
BGLN423
BGLU472
BLEU473

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO B 606
ChainResidue
BLEU524
BHIS530
BARG535
CGLU525

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO B 607
ChainResidue
BLYS428
BSER432
BLEU455

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO C 602
ChainResidue
CSER513
CHIS547
CSER548

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO C 603
ChainResidue
CHIS516
CARG517

site_idAD3
Number of Residues2
Detailsbinding site for residue EDO C 604
ChainResidue
CTRP420
CGLU469

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO D 601
ChainResidue
DGLY425
DPHE426
DTYR429
DARG465
EGLN437

site_idAD5
Number of Residues8
Detailsbinding site for residue PEG D 602
ChainResidue
DALA477
DASN478
DTYR479
DSER480
DASP483
DASN486
DALA488
DARG499

site_idAD6
Number of Residues2
Detailsbinding site for residue EDO D 604
ChainResidue
DASP489
DARG512

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO D 605
ChainResidue
DLYS428
DSER432
DLEU455

site_idAD8
Number of Residues2
Detailsbinding site for residue EDO D 606
ChainResidue
DGLU448
DARG463

site_idAD9
Number of Residues5
Detailsbinding site for residue EDO D 607
ChainResidue
DGLN452
DLYS458
DARG463
EGLU449
EASP454

site_idAE1
Number of Residues4
Detailsbinding site for residue EDO D 608
ChainResidue
DARG465
DARG468
EGLN437
EASP439

site_idAE2
Number of Residues7
Detailsbinding site for residue EDO E 601
ChainResidue
DGLU520
DGLY532
DARG535
EGLN521
EGLN522
EGLU525
EASP526

site_idAE3
Number of Residues3
Detailsbinding site for residue EDO F 601
ChainResidue
ESER459
FGLN436
FASP454

site_idAE4
Number of Residues5
Detailsbinding site for Di-peptide BME B 604 and CYS B 482
ChainResidue
BTYR479
BSER480
BTHR481
BASP483
BVAL506

site_idAE5
Number of Residues6
Detailsbinding site for Di-peptide BME C 601 and CYS C 482
ChainResidue
CTYR479
CSER480
CTHR481
CASP483
CTYR503
CVAL506

site_idAE6
Number of Residues7
Detailsbinding site for Di-peptide BME D 603 and CYS D 482
ChainResidue
DTHR481
DASP483
DVAL506
DSER507
CARG497
DTYR479
DSER480

site_idAE7
Number of Residues6
Detailsbinding site for Di-peptide BME E 602 and CYS E 482
ChainResidue
ETYR479
ESER480
ETHR481
EASP483
EVAL506
ESER507

site_idAE8
Number of Residues7
Detailsbinding site for Di-peptide BME F 602 and CYS F 482
ChainResidue
FTYR479
FSER480
FTHR481
FASP483
FTYR503
FVAL506
FSER507

site_idAE9
Number of Residues6
Detailsbinding site for Di-peptide BME G 601 and CYS G 482
ChainResidue
GTYR479
GSER480
GTHR481
GASP483
GVAL506
GSER507

site_idAF1
Number of Residues7
Detailsbinding site for Di-peptide BME H 601 and CYS H 482
ChainResidue
HTYR479
HSER480
HTHR481
HASP483
HARG484
HVAL506
HSER507

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:30333228
ChainResidueDetails
ASER548
BSER548
CSER548
DSER548
ESER548
FSER548
GSER548
HSER548

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PDB entries from 2024-07-17

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