4DNC
Crystal structure of human MOF in complex with MSL1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004402 | molecular_function | histone acetyltransferase activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0004402 | molecular_function | histone acetyltransferase activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0072487 | cellular_component | MSL complex |
E | 0072487 | cellular_component | MSL complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | CYS210 |
A | CYS213 |
A | HIS226 |
A | CYS230 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 501 |
Chain | Residue |
B | CYS210 |
B | CYS213 |
B | HIS226 |
B | CYS230 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 50 |
Details | Zinc finger: {"description":"C2HC MYST-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27768893","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33657400","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PQ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DNC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22547026","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22918831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 36 |
Details | Region: {"description":"Interaction with KAT8 HAT domain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01397","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 28 |
Details | Motif: {"description":"Bipartite nuclear localization signal","evidences":[{"source":"UniProtKB","id":"Q6PDM1","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |