9PC3
21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 12
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 72 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"9731775","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9727495","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"9731775","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P46460","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphoserine; by CDK16","evidences":[{"source":"UniProtKB","id":"P46460","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P46460","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P46459","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C)","evidences":[{"source":"PubMed","id":"7737992","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"UniProtKB","id":"Q16623","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 62 |
Details | Domain: {"description":"t-SNARE coiled-coil homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"PubMed","id":"12730201","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 62 |
Details | Domain: {"description":"t-SNARE coiled-coil homology 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 62 |
Details | Domain: {"description":"t-SNARE coiled-coil homology 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 74 |
Details | Region: {"description":"Interaction with CENPF","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 22 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 19 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E)","evidences":[{"source":"PubMed","id":"8243676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8294407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8103915","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA)","evidences":[{"source":"PubMed","id":"8243676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8294407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8103915","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by PKC and PKA","evidences":[{"source":"PubMed","id":"12459461","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60879","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"12459461","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI21 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P54920","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI22 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DB05","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI23 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P54920","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
A | LYS549 | electrostatic stabiliser |
A | THR550 | electrostatic stabiliser |
A | ASP603 | electrostatic stabiliser |
A | ASP604 | proton acceptor |
A | LYS631 | electrostatic stabiliser |
A | LYS708 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
B | LYS549 | electrostatic stabiliser |
B | THR550 | electrostatic stabiliser |
B | ASP603 | electrostatic stabiliser |
B | ASP604 | proton acceptor |
B | LYS631 | electrostatic stabiliser |
B | LYS708 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
C | LYS549 | electrostatic stabiliser |
C | THR550 | electrostatic stabiliser |
C | ASP603 | electrostatic stabiliser |
C | ASP604 | proton acceptor |
C | LYS631 | electrostatic stabiliser |
C | LYS708 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
D | LYS549 | electrostatic stabiliser |
D | THR550 | electrostatic stabiliser |
D | ASP603 | electrostatic stabiliser |
D | ASP604 | proton acceptor |
D | LYS631 | electrostatic stabiliser |
D | LYS708 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
E | LYS549 | electrostatic stabiliser |
E | THR550 | electrostatic stabiliser |
E | ASP603 | electrostatic stabiliser |
E | ASP604 | proton acceptor |
E | LYS631 | electrostatic stabiliser |
E | LYS708 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
F | LYS549 | electrostatic stabiliser |
F | THR550 | electrostatic stabiliser |
F | ASP603 | electrostatic stabiliser |
F | ASP604 | proton acceptor |
F | LYS631 | electrostatic stabiliser |
F | LYS708 | electrostatic stabiliser |