4EZH
the crystal structure of KDM6B bound with H3K27me3 peptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071557 | biological_process | histone H3-K27 demethylation |
| A | 0071558 | molecular_function | histone H3-tri/di-methyl-lysine-27 demethylase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071557 | biological_process | histone H3-K27 demethylation |
| B | 0071558 | molecular_function | histone H3-tri/di-methyl-lysine-27 demethylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 1701 |
| Chain | Residue |
| A | HIS1390 |
| A | GLU1392 |
| A | HIS1470 |
| A | OGA1703 |
| A | HOH1813 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1702 |
| Chain | Residue |
| A | CYS1575 |
| A | CYS1578 |
| A | CYS1602 |
| A | CYS1605 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OGA A 1703 |
| Chain | Residue |
| A | LYS1381 |
| A | THR1387 |
| A | HIS1390 |
| A | GLU1392 |
| A | SER1398 |
| A | ASN1400 |
| A | HIS1470 |
| A | ALA1482 |
| A | NI1701 |
| A | HOH1801 |
| A | HOH1813 |
| C | M3L27 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 1701 |
| Chain | Residue |
| B | HIS1390 |
| B | GLU1392 |
| B | HIS1470 |
| B | OGA1703 |
| B | HOH1811 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1702 |
| Chain | Residue |
| B | CYS1575 |
| B | CYS1578 |
| B | CYS1602 |
| B | CYS1605 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE OGA B 1703 |
| Chain | Residue |
| B | LYS1381 |
| B | THR1387 |
| B | HIS1390 |
| B | GLU1392 |
| B | SER1398 |
| B | ASN1400 |
| B | HIS1470 |
| B | NI1701 |
| B | HOH1802 |
| B | HOH1811 |
| D | M3L27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 326 |
| Details | Domain: {"description":"JmjC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O14607","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5","evidences":[{"source":"PubMed","id":"10464286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11856369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15681610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15684425","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16457588","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
