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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:20726530 |
Chain | Residue | Details |
A | HIS135 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 |
Chain | Residue | Details |
A | GLY32 | |
A | GLN115 | |
A | GLY223 | |
A | ASN248 | |
A | SER270 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592 |
Chain | Residue | Details |
A | CYS143 | |
A | CYS146 | |
A | CYS170 | |
A | CYS173 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | SER2 |
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 |