6LYF
Crystal structure of the mouse endonuclease EndoG(H138A/Se-Met)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASN169 |
| A | HOH406 |
| A | HOH410 |
| A | HOH417 |
| A | HOH422 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASN169 |
| B | HOH426 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 301 |
| Chain | Residue |
| C | HOH419 |
| C | HOH426 |
| C | HOH429 |
| C | ASN169 |
| C | HOH417 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 301 |
| Chain | Residue |
| D | GLY137 |
| D | ALA138 |
| D | GLN164 |
| D | ASN169 |
| D | TRP173 |
| D | HOH416 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10047, ECO:0000269|PubMed:32095813, ECO:0000269|PubMed:32192768 |
| Chain | Residue | Details |
| A | ALA138 | |
| B | ALA138 | |
| C | ALA138 | |
| D | ALA138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:32095813, ECO:0000269|PubMed:32192768, ECO:0007744|PDB:6LYF, ECO:0007744|PDB:6NJT |
| Chain | Residue | Details |
| A | ASN169 | |
| B | ASN169 | |
| C | ASN169 | |
| D | ASN169 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Essential for catalytic activity => ECO:0000269|PubMed:32192768 |
| Chain | Residue | Details |
| A | ARG107 | |
| B | ARG107 | |
| C | ARG107 | |
| D | ARG107 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14249 |
| Chain | Residue | Details |
| A | THR125 | |
| B | THR125 | |
| C | THR125 | |
| D | THR125 |
