5DWQ
Crystal structure of CARM1, sinefungin, and methylated H3 peptide (R17)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
A | 0018216 | biological_process | peptidyl-arginine methylation |
B | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
B | 0018216 | biological_process | peptidyl-arginine methylation |
C | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
C | 0018216 | biological_process | peptidyl-arginine methylation |
D | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
D | 0018216 | biological_process | peptidyl-arginine methylation |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0030527 | molecular_function | structural constituent of chromatin |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0030527 | molecular_function | structural constituent of chromatin |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | binding site for residue SFG A 501 |
Chain | Residue |
A | TYR149 |
A | GLU214 |
A | ALA215 |
A | LYS241 |
A | VAL242 |
A | GLU243 |
A | GLU257 |
A | MET268 |
A | SER271 |
A | HOH602 |
A | HOH614 |
A | PHE150 |
A | HOH624 |
A | HOH628 |
A | HOH642 |
A | TYR153 |
A | GLN159 |
A | MET162 |
A | ARG168 |
A | CYS193 |
A | ILE197 |
A | LEU198 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | HOH637 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue SFG B 501 |
Chain | Residue |
B | TYR149 |
B | PHE150 |
B | TYR153 |
B | GLN159 |
B | MET162 |
B | ARG168 |
B | CYS193 |
B | ILE197 |
B | LEU198 |
B | GLU214 |
B | ALA215 |
B | LYS241 |
B | VAL242 |
B | GLU243 |
B | GLU257 |
B | MET268 |
B | SER271 |
B | HOH602 |
B | HOH609 |
B | HOH637 |
B | HOH650 |
F | NMM5 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
A | GLN151 |
B | GLN148 |
B | ARG445 |
B | LYS470 |
B | HOH611 |
F | LYS2 |
site_id | AC5 |
Number of Residues | 19 |
Details | binding site for residue SFG C 501 |
Chain | Residue |
C | TYR149 |
C | PHE150 |
C | TYR153 |
C | GLN159 |
C | MET162 |
C | ARG168 |
C | CYS193 |
C | ILE197 |
C | GLU214 |
C | ALA215 |
C | LYS241 |
C | VAL242 |
C | GLU243 |
C | GLU257 |
C | MET268 |
C | SER271 |
C | HOH601 |
C | HOH608 |
C | HOH617 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
C | GLU266 |
site_id | AC7 |
Number of Residues | 21 |
Details | binding site for residue SFG D 501 |
Chain | Residue |
D | TYR149 |
D | TYR153 |
D | GLN159 |
D | MET162 |
D | ARG168 |
D | CYS193 |
D | ILE197 |
D | LEU198 |
D | GLU214 |
D | ALA215 |
D | LYS241 |
D | VAL242 |
D | GLU243 |
D | GLU257 |
D | MET268 |
D | SER271 |
D | HOH608 |
D | HOH611 |
D | HOH613 |
D | HOH640 |
G | NMM5 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 502 |
Chain | Residue |
C | GLN151 |
D | GLN148 |
D | ARG445 |
D | LYS470 |
G | LYS2 |
G | HOH102 |
Functional Information from PROSITE/UniProt
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
F | LYS2-LEU8 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
D | GLY192 | |
D | GLU214 | |
D | GLU243 | |
D | SER271 | |
F | LYS2 | |
G | LYS2 | |
A | GLY192 | |
A | GLU214 | |
A | GLU243 | |
A | SER271 | |
B | GLN159 | |
B | ARG168 | |
B | GLY192 | |
B | GLU214 | |
B | GLU243 | |
B | SER271 | |
C | GLN159 | |
C | ARG168 | |
C | GLY192 | |
C | GLU214 | |
C | GLU243 | |
C | SER271 | |
D | GLN159 | |
D | ARG168 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635 |
Chain | Residue | Details |
F | NMM5 | |
G | NMM5 | |
C | SER216 | |
D | SER216 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
B | LYS227 | |
C | LYS227 | |
D | LYS227 | |
F | LYS6 | |
G | LYS6 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
F | LYS11 | |
G | LYS11 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline => ECO:0000269|PubMed:16567635 |
Chain | Residue | Details |
F | ARG14 | |
G | ARG14 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:7309716 |
Chain | Residue | Details |
F | LYS15 | |
G | LYS15 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15851689, ECO:0000269|PubMed:16185088 |
Chain | Residue | Details |
F | SER16 | |
G | SER16 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | LIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806 |
Chain | Residue | Details |
F | LYS6 | |
G | LYS6 |