6YDF
X-ray structure of LPMO.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030245 | biological_process | cellulose catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030245 | biological_process | cellulose catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CU A 301 |
| Chain | Residue |
| A | HIS79 |
| A | GLN167 |
| A | TYR169 |
| A | HIC302 |
| A | HOH498 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue HIC A 302 |
| Chain | Residue |
| A | ILE74 |
| A | ILE75 |
| A | HIS79 |
| A | TYR169 |
| A | CU301 |
| A | HOH457 |
| A | THR2 |
| A | THR28 |
| A | ASP29 |
| A | ARG67 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | HIS79 |
| A | HIS152 |
| A | GLU153 |
| A | GLN167 |
| A | HOH417 |
| A | HOH452 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | LYS197 |
| A | TYR198 |
| A | SER199 |
| A | HOH432 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CU B 301 |
| Chain | Residue |
| B | HIS79 |
| B | GLN167 |
| B | TYR169 |
| B | HIC302 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | LYS197 |
| B | TYR198 |
| B | SER199 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide HIC B 302 and THR B 2 |
| Chain | Residue |
| B | ARG3 |
| B | THR28 |
| B | ASP29 |
| B | TYR66 |
| B | ARG67 |
| B | ILE74 |
| B | ILE75 |
| B | HIS79 |
| B | TYR169 |
| B | CU301 |
| B | HOH427 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0007744|PDB:5NLT, ECO:0007744|PDB:6YDC, ECO:0007744|PDB:6YDD, ECO:0007744|PDB:6YDE, ECO:0007744|PDB:6YDF |
| Chain | Residue | Details |
| A | HIC302 | |
| A | HIS79 | |
| A | TYR169 | |
| B | HIC302 | |
| B | HIS79 | |
| B | TYR169 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDE |
| Chain | Residue | Details |
| A | GLY45 | |
| B | GLY45 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDC, ECO:0007744|PDB:6YDD, ECO:0007744|PDB:6YDE |
| Chain | Residue | Details |
| A | ASP76 | |
| A | SER78 | |
| A | ASP155 | |
| B | ASP76 | |
| B | SER78 | |
| B | ASP155 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q1K8B6 |
| Chain | Residue | Details |
| A | HIS152 | |
| B | HIS152 |
