5YKN
crystal structure of Arabidopsis thaliana JMJ14 catalytic domain
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue NI A 800 |
| Chain | Residue |
| A | HIS309 |
| A | GLU311 |
| A | HIS397 |
| A | HOH997 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 801 |
| Chain | Residue |
| A | CYS519 |
| A | CYS522 |
| A | CYS542 |
| A | HIS545 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 802 |
| Chain | Residue |
| A | CYS535 |
| A | CYS550 |
| A | CYS552 |
| A | CYS533 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 52 |
| Details | ZN_FING: C5HC2 => ECO:0000255 |
| Chain | Residue | Details |
| A | CYS519-LEU571 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO |
| Chain | Residue | Details |
| A | HIS309 | |
| A | GLU311 | |
| A | HIS397 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO |
| Chain | Residue | Details |
| A | CYS519 | |
| A | CYS522 | |
| A | CYS542 | |
| A | HIS545 | |
| A | CYS533 | |
| A | CYS535 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKO |
| Chain | Residue | Details |
| A | CYS550 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN |
| Chain | Residue | Details |
| A | CYS552 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Involved in histone H3A7 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO |
| Chain | Residue | Details |
| A | VAL363 | |
| A | PHE171 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Involved in histone H3R2 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO |
| Chain | Residue | Details |
| A | GLU285 | |
| A | GLU516 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Involved in histone H3K4me3 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO |
| Chain | Residue | Details |
| A | SER290 | |
| A | TYR298 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | SITE: Involved in histone H3Q5 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO |
| Chain | Residue | Details |
| A | ASP312 |
