6QWV
SARM1 SAM1-2 domains
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003953 | molecular_function | NAD+ nucleosidase activity |
| A | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| A | 0035591 | molecular_function | signaling adaptor activity |
| A | 0048678 | biological_process | response to axon injury |
| B | 0003953 | molecular_function | NAD+ nucleosidase activity |
| B | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| B | 0035591 | molecular_function | signaling adaptor activity |
| B | 0048678 | biological_process | response to axon injury |
| C | 0003953 | molecular_function | NAD+ nucleosidase activity |
| C | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| C | 0035591 | molecular_function | signaling adaptor activity |
| C | 0048678 | biological_process | response to axon injury |
| D | 0003953 | molecular_function | NAD+ nucleosidase activity |
| D | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| D | 0035591 | molecular_function | signaling adaptor activity |
| D | 0048678 | biological_process | response to axon injury |
| E | 0003953 | molecular_function | NAD+ nucleosidase activity |
| E | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| E | 0035591 | molecular_function | signaling adaptor activity |
| E | 0048678 | biological_process | response to axon injury |
| F | 0003953 | molecular_function | NAD+ nucleosidase activity |
| F | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| F | 0035591 | molecular_function | signaling adaptor activity |
| F | 0048678 | biological_process | response to axon injury |
| G | 0003953 | molecular_function | NAD+ nucleosidase activity |
| G | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| G | 0035591 | molecular_function | signaling adaptor activity |
| G | 0048678 | biological_process | response to axon injury |
| H | 0003953 | molecular_function | NAD+ nucleosidase activity |
| H | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| H | 0035591 | molecular_function | signaling adaptor activity |
| H | 0048678 | biological_process | response to axon injury |
| I | 0003953 | molecular_function | NAD+ nucleosidase activity |
| I | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| I | 0035591 | molecular_function | signaling adaptor activity |
| I | 0048678 | biological_process | response to axon injury |
| J | 0003953 | molecular_function | NAD+ nucleosidase activity |
| J | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| J | 0035591 | molecular_function | signaling adaptor activity |
| J | 0048678 | biological_process | response to axon injury |
| K | 0003953 | molecular_function | NAD+ nucleosidase activity |
| K | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| K | 0035591 | molecular_function | signaling adaptor activity |
| K | 0048678 | biological_process | response to axon injury |
| L | 0003953 | molecular_function | NAD+ nucleosidase activity |
| L | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| L | 0035591 | molecular_function | signaling adaptor activity |
| L | 0048678 | biological_process | response to axon injury |
| M | 0003953 | molecular_function | NAD+ nucleosidase activity |
| M | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| M | 0035591 | molecular_function | signaling adaptor activity |
| M | 0048678 | biological_process | response to axon injury |
| N | 0003953 | molecular_function | NAD+ nucleosidase activity |
| N | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| N | 0035591 | molecular_function | signaling adaptor activity |
| N | 0048678 | biological_process | response to axon injury |
| O | 0003953 | molecular_function | NAD+ nucleosidase activity |
| O | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| O | 0035591 | molecular_function | signaling adaptor activity |
| O | 0048678 | biological_process | response to axon injury |
| P | 0003953 | molecular_function | NAD+ nucleosidase activity |
| P | 0034128 | biological_process | negative regulation of MyD88-independent toll-like receptor signaling pathway |
| P | 0035591 | molecular_function | signaling adaptor activity |
| P | 0048678 | biological_process | response to axon injury |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 601 |
| Chain | Residue |
| A | LYS428 |
| A | SER432 |
| A | LEU455 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue BME A 602 |
| Chain | Residue |
| A | CYS482 |
| A | TYR503 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | GLY425 |
| A | LYS428 |
| A | ARG465 |
| B | GLN437 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 601 |
| Chain | Residue |
| B | LEU444 |
| B | GLY504 |
| B | HOH725 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| B | ALA477 |
| B | ASN478 |
| B | TYR479 |
| B | SER480 |
| B | ASP483 |
| B | ASN486 |
| B | ALA488 |
| B | ARG499 |
| M | HOH720 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 603 |
| Chain | Residue |
| B | ARG497 |
| B | GLN500 |
| B | HIS534 |
| C | SER507 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue PGE B 605 |
| Chain | Residue |
| B | PRO402 |
| B | ARG403 |
| B | PRO404 |
| B | TRP412 |
| B | GLU416 |
| B | TRP420 |
| B | GLN423 |
| B | GLU472 |
| B | LEU473 |
| B | HOH751 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 606 |
| Chain | Residue |
| B | LEU524 |
| B | HIS530 |
| B | ARG535 |
| B | HOH718 |
| C | GLU525 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 607 |
| Chain | Residue |
| B | LYS428 |
| B | SER432 |
| B | LEU455 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 602 |
| Chain | Residue |
| C | SER432 |
| C | SER513 |
| C | HIS547 |
| C | SER548 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 603 |
| Chain | Residue |
| C | HIS516 |
| C | ARG517 |
| C | HOH746 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 604 |
| Chain | Residue |
| C | TRP420 |
| C | GLU469 |
| F | ILE405 |
| F | LEU406 |
| F | HOH712 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 601 |
| Chain | Residue |
| D | GLY425 |
| D | PHE426 |
| D | TYR429 |
| D | ARG465 |
| D | HOH715 |
| D | HOH757 |
| E | GLN437 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue PEG D 602 |
| Chain | Residue |
| D | ALA477 |
| D | ASN478 |
| D | TYR479 |
| D | SER480 |
| D | ASP483 |
| D | ASN486 |
| D | ALA488 |
| D | ARG499 |
| E | PHE476 |
| E | PRO496 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 604 |
| Chain | Residue |
| D | ASP489 |
| D | ARG512 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 605 |
| Chain | Residue |
| D | LYS428 |
| D | SER432 |
| D | LEU455 |
| D | HIS516 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 606 |
| Chain | Residue |
| D | GLU448 |
| D | ARG463 |
| D | HOH732 |
| E | HOH707 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 607 |
| Chain | Residue |
| D | GLN452 |
| D | LYS458 |
| D | ARG463 |
| E | GLU449 |
| E | ASP454 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 608 |
| Chain | Residue |
| D | ARG465 |
| D | ARG468 |
| E | GLN437 |
| E | ASP439 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO E 601 |
| Chain | Residue |
| D | GLU520 |
| D | GLY532 |
| D | ARG535 |
| E | GLN521 |
| E | GLN522 |
| E | GLU525 |
| E | ASP526 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO F 601 |
| Chain | Residue |
| F | GLN436 |
| F | ASP454 |
| F | HOH721 |
| E | SER459 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO I 601 |
| Chain | Residue |
| I | GLU449 |
| I | GLU450 |
| I | ASP454 |
| I | HOH704 |
| I | HOH738 |
| J | GLY460 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO I 602 |
| Chain | Residue |
| I | ASN478 |
| I | TYR479 |
| I | SER480 |
| I | ASP483 |
| I | ASN486 |
| I | ALA488 |
| I | ARG499 |
| site_id | AE6 |
| Number of Residues | 11 |
| Details | binding site for residue PEG J 601 |
| Chain | Residue |
| I | GLN437 |
| I | HOH717 |
| J | GLY425 |
| J | PHE426 |
| J | LYS428 |
| J | TYR429 |
| J | THR462 |
| J | ARG465 |
| J | HOH702 |
| J | HOH745 |
| J | HOH770 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue PEG J 602 |
| Chain | Residue |
| J | PRO404 |
| J | TRP412 |
| J | GLU416 |
| J | THR419 |
| J | GLN423 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO J 603 |
| Chain | Residue |
| J | LEU446 |
| J | HOH718 |
| J | HOH744 |
| site_id | AE9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO J 604 |
| Chain | Residue |
| I | PHE476 |
| J | ASN478 |
| J | TYR479 |
| J | SER480 |
| J | ASP483 |
| J | ASN486 |
| J | ALA488 |
| J | ARG499 |
| site_id | AF1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO J 605 |
| Chain | Residue |
| J | LEU444 |
| J | TYR503 |
| J | GLY504 |
| J | HOH710 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO J 607 |
| Chain | Residue |
| J | LEU455 |
| J | GLY456 |
| J | HIS516 |
| J | EDO608 |
| J | HOH726 |
| site_id | AF3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO J 608 |
| Chain | Residue |
| J | LYS428 |
| J | HIS516 |
| J | EDO607 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO J 609 |
| Chain | Residue |
| J | GLN500 |
| J | HIS534 |
| J | HOH737 |
| J | HOH755 |
| site_id | AF5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO K 601 |
| Chain | Residue |
| K | PHE467 |
| site_id | AF6 |
| Number of Residues | 6 |
| Details | binding site for residue PEG K 603 |
| Chain | Residue |
| K | PRO407 |
| K | SER408 |
| K | SER411 |
| K | TRP412 |
| K | LYS413 |
| K | GLU416 |
| site_id | AF7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO K 604 |
| Chain | Residue |
| K | ASP439 |
| K | HOH709 |
| site_id | AF8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO K 605 |
| Chain | Residue |
| K | ASN478 |
| K | TYR479 |
| K | SER480 |
| K | ASP483 |
| K | ASN486 |
| K | ALA488 |
| K | ARG499 |
| site_id | AF9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO K 606 |
| Chain | Residue |
| K | LEU514 |
| K | ARG517 |
| K | GLN522 |
| K | HOH722 |
| site_id | AG1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO L 601 |
| Chain | Residue |
| L | LYS428 |
| L | SER432 |
| L | LEU455 |
| L | GLY456 |
| site_id | AG2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO L 603 |
| Chain | Residue |
| L | ASP454 |
| L | HIS547 |
| site_id | AG3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO L 604 |
| Chain | Residue |
| L | HIS530 |
| L | ARG535 |
| site_id | AG4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO M 602 |
| Chain | Residue |
| M | SER411 |
| M | LYS413 |
| M | GLU416 |
| site_id | AG5 |
| Number of Residues | 10 |
| Details | binding site for residue EDO M 603 |
| Chain | Residue |
| B | ASN478 |
| B | HOH732 |
| M | ALA477 |
| M | ASN478 |
| M | TYR479 |
| M | SER480 |
| M | ASP483 |
| M | ASN486 |
| M | ALA488 |
| M | ARG499 |
| site_id | AG6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO M 604 |
| Chain | Residue |
| B | PRO404 |
| M | ARG512 |
| site_id | AG7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO M 605 |
| Chain | Residue |
| M | GLN500 |
| M | HIS534 |
| M | HOH719 |
| site_id | AG8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO N 602 |
| Chain | Residue |
| N | GLU448 |
| N | PHE467 |
| site_id | AG9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO O 601 |
| Chain | Residue |
| H | GLU416 |
| O | ARG512 |
| O | HOH714 |
| site_id | AH1 |
| Number of Residues | 1 |
| Details | binding site for residue EDO O 603 |
| Chain | Residue |
| O | HOH708 |
| site_id | AH2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO O 604 |
| Chain | Residue |
| O | LEU446 |
| O | PHE467 |
| O | LYS474 |
| site_id | AH3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO P 601 |
| Chain | Residue |
| O | GLN437 |
| P | GLY425 |
| P | ARG465 |
| site_id | AH4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO P 602 |
| Chain | Residue |
| P | LYS428 |
| P | SER432 |
| P | LEU455 |
| P | GLY456 |
| site_id | AH5 |
| Number of Residues | 6 |
| Details | binding site for residue PGE P 604 |
| Chain | Residue |
| I | ARG468 |
| P | ASP439 |
| P | ASP441 |
| P | ARG445 |
| P | SER507 |
| P | BME603 |
| site_id | AH6 |
| Number of Residues | 1 |
| Details | binding site for residue EDO P 605 |
| Chain | Residue |
| P | ARG445 |
| site_id | AH7 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide BME B 604 and CYS B 482 |
| Chain | Residue |
| B | TYR479 |
| B | SER480 |
| B | THR481 |
| B | ASP483 |
| B | VAL506 |
| B | HOH738 |
| site_id | AH8 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BME C 601 and CYS C 482 |
| Chain | Residue |
| C | TYR479 |
| C | SER480 |
| C | THR481 |
| C | ASP483 |
| C | TYR503 |
| C | VAL506 |
| C | HOH706 |
| site_id | AH9 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BME D 603 and CYS D 482 |
| Chain | Residue |
| C | ARG497 |
| D | TYR479 |
| D | SER480 |
| D | THR481 |
| D | ASP483 |
| D | VAL506 |
| D | SER507 |
| site_id | AI1 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide BME E 602 and CYS E 482 |
| Chain | Residue |
| E | TYR479 |
| E | SER480 |
| E | THR481 |
| E | ASP483 |
| E | VAL506 |
| E | SER507 |
| site_id | AI2 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BME F 602 and CYS F 482 |
| Chain | Residue |
| F | TYR479 |
| F | SER480 |
| F | THR481 |
| F | ASP483 |
| F | TYR503 |
| F | VAL506 |
| F | SER507 |
| site_id | AI3 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide BME G 601 and CYS G 482 |
| Chain | Residue |
| G | TYR479 |
| G | SER480 |
| G | THR481 |
| G | ASP483 |
| G | VAL506 |
| G | SER507 |
| site_id | AI4 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BME H 601 and CYS H 482 |
| Chain | Residue |
| H | TYR479 |
| H | SER480 |
| H | THR481 |
| H | ASP483 |
| H | ARG484 |
| H | VAL506 |
| H | SER507 |
| site_id | AI5 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide BME I 603 and CYS I 482 |
| Chain | Residue |
| I | TYR479 |
| I | SER480 |
| I | THR481 |
| I | ASP483 |
| I | TYR503 |
| I | VAL506 |
| site_id | AI6 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide BME J 606 and CYS J 482 |
| Chain | Residue |
| J | TYR479 |
| J | SER480 |
| J | THR481 |
| J | ASP483 |
| J | TYR503 |
| J | VAL506 |
| J | SER507 |
| J | HOH733 |
| P | ARG484 |
| site_id | AI7 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BME K 602 and CYS K 482 |
| Chain | Residue |
| K | TYR479 |
| K | SER480 |
| K | THR481 |
| K | ASP483 |
| K | TYR503 |
| K | VAL506 |
| K | HOH707 |
| site_id | AI8 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide BME L 602 and CYS L 482 |
| Chain | Residue |
| L | TYR479 |
| L | SER480 |
| L | THR481 |
| L | ASP483 |
| L | VAL506 |
| L | SER507 |
| site_id | AI9 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide BME M 601 and CYS M 482 |
| Chain | Residue |
| M | TYR479 |
| M | SER480 |
| M | THR481 |
| M | ASP483 |
| M | VAL506 |
| M | SER507 |
| site_id | AJ1 |
| Number of Residues | 5 |
| Details | binding site for Di-peptide BME N 601 and CYS N 482 |
| Chain | Residue |
| N | TYR479 |
| N | SER480 |
| N | THR481 |
| N | ASP483 |
| N | VAL506 |
| site_id | AJ2 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BME O 602 and CYS O 482 |
| Chain | Residue |
| O | TYR479 |
| O | SER480 |
| O | THR481 |
| O | ASP483 |
| O | TYR503 |
| O | VAL506 |
| O | SER507 |
| site_id | AJ3 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide BME P 603 and CYS P 482 |
| Chain | Residue |
| J | ARG484 |
| P | TYR479 |
| P | SER480 |
| P | THR481 |
| P | ASP483 |
| P | VAL506 |
| P | SER507 |
| P | PGE604 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1024 |
| Details | Domain: {"description":"SAM 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00184","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 434 |
| Details | Domain: {"description":"SAM 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00184","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"30333228","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
