2XM1
BtGH84 in complex with N-acetyl gluconolactam
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006517 | biological_process | protein deglycosylation |
| A | 0015929 | molecular_function | hexosaminidase activity |
| A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006517 | biological_process | protein deglycosylation |
| B | 0015929 | molecular_function | hexosaminidase activity |
| B | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1716 |
| Chain | Residue |
| A | TYR137 |
| A | ASP344 |
| A | TYR345 |
| A | ARG347 |
| A | GLN551 |
| A | HOH2523 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE LTM B 1716 |
| Chain | Residue |
| B | ASP242 |
| B | ASP243 |
| B | TYR282 |
| B | VAL314 |
| B | TRP337 |
| B | ASN339 |
| B | ASP344 |
| B | TYR345 |
| B | ASN372 |
| B | HOH2391 |
| B | HOH2516 |
| B | GLY135 |
| B | PHE136 |
| B | LYS166 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE LTM A 1717 |
| Chain | Residue |
| A | GLY135 |
| A | PHE136 |
| A | LYS166 |
| A | ASP242 |
| A | ASP243 |
| A | TYR282 |
| A | VAL314 |
| A | TRP337 |
| A | ASN339 |
| A | ASP344 |
| A | TYR345 |
| A | ASN372 |
| A | HOH2524 |
| A | HOH2525 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1717 |
| Chain | Residue |
| B | GLN501 |
| B | PHE539 |
| B | VAL554 |
| B | LYS555 |
| B | ASP589 |
| B | HOH2479 |
| B | HOH2517 |
| B | HOH2518 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 1718 |
| Chain | Residue |
| B | ASP243 |
| B | SER245 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1718 |
| Chain | Residue |
| A | GLN501 |
| A | PHE539 |
| A | VAL554 |
| A | LYS555 |
| A | ASP589 |
| A | HOH2476 |
| A | HOH2526 |
| A | HOH2527 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 534 |
| Details | Domain: {"description":"GH84","evidences":[{"source":"PROSITE-ProRule","id":"PRU01353","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 570 |
| Details | Region: {"description":"Catalytic domain","evidences":[{"source":"PubMed","id":"16565725","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01353","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16565725","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16565725","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
