2OD2
Crystal Structure of yHst2 I117F mutant bound to carba-NAD+ and an acetylated H4 peptide
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | CYS143 |
| A | CYS146 |
| A | CYS170 |
| A | CYS173 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CNA A 1001 |
| Chain | Residue |
| A | GLN115 |
| A | ASN116 |
| A | PHE117 |
| A | ASP118 |
| A | GLY223 |
| A | THR224 |
| A | SER225 |
| A | ASN248 |
| A | LEU249 |
| A | GLN268 |
| A | TYR269 |
| A | SER270 |
| A | HOH2011 |
| A | HOH2015 |
| A | HOH2030 |
| A | HOH2076 |
| A | HOH2092 |
| A | HOH2095 |
| A | HOH2119 |
| B | ALY16 |
| A | GLY32 |
| A | ALA33 |
| A | GLY34 |
| A | THR37 |
| A | ARG45 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1989 |
| Chain | Residue |
| A | SER193 |
| A | TRP196 |
| A | GLU237 |
| B | LYS12 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1990 |
| Chain | Residue |
| A | THR49 |
| A | GLY50 |
| A | HOH2004 |
| A | HOH2090 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1991 |
| Chain | Residue |
| A | LYS84 |
| A | TYR87 |
| A | ASN90 |
| A | LEU159 |
| A | ALA160 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1992 |
| Chain | Residue |
| A | LYS26 |
| A | LYS110 |
| A | TRP202 |
| A | LYS206 |
Functional Information from PROSITE/UniProt
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| B | GLY14-HIS18 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20726530","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14604530","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 240 |
| Chain | Residue | Details |
| A | PRO42 | hydrogen bond acceptor, steric role |
| A | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
| A | PHE44 | steric role, van der waals interaction |
| A | ARG45 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
| A | ASP118 | activator, hydrogen bond acceptor |
| A | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
