5YKO
Crystal structure of Arabidopsis thaliana JMJ14 catalytic domain in complex with NOG and H3K4me3 peptide
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 | OGA803 |
| 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 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue OGA A 803 |
| Chain | Residue |
| A | TYR236 |
| A | TYR298 |
| A | PHE306 |
| A | HIS309 |
| A | GLU311 |
| A | SER317 |
| A | ASN319 |
| A | LYS327 |
| A | TRP329 |
| A | HIS397 |
| A | ALA409 |
| A | NI800 |
| P | M3L4 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16258034 |
| Chain | Residue | Details |
| P | M3L4 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12456661, ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15014946, ECO:0000269|PubMed:15598823 |
| Chain | Residue | Details |
| P | LYS9 | |
| A | GLU311 | |
| A | HIS397 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 |
| Chain | Residue | Details |
| P | SER10 | |
| A | CYS522 | |
| A | CYS533 | |
| A | CYS535 | |
| A | CYS542 | |
| A | HIS545 |
| 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 | PHE171 | |
| A | VAL363 |
| 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 |
