4L1G
Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase from Bacillus cereus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | HIS231 |
| A | LEU232 |
| A | GLN233 |
| A | HOH561 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 302 |
| Chain | Residue |
| A | TRP193 |
| A | HIS225 |
| A | ASP80 |
| A | HIS135 |
| A | PRO170 |
| A | PXU171 |
| A | TYR172 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 301 |
| Chain | Residue |
| B | HIS231 |
| B | LEU232 |
| B | GLN233 |
| B | HOH546 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT B 302 |
| Chain | Residue |
| B | ASP80 |
| B | ASP81 |
| B | HIS131 |
| B | HIS135 |
| B | PXU171 |
| B | TYR172 |
| B | HIS225 |
| B | HOH509 |
| B | HOH583 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 301 |
| Chain | Residue |
| A | ASN99 |
| A | LYS247 |
| C | HIS98 |
| C | PRO244 |
| C | LYS247 |
| C | HOH420 |
| C | HOH441 |
| C | HOH463 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| C | HIS231 |
| C | LEU232 |
| C | GLN233 |
| C | HOH454 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT C 303 |
| Chain | Residue |
| C | ASP80 |
| C | PRO170 |
| C | PXU171 |
| C | TYR172 |
| C | TRP193 |
| C | HIS225 |
| C | HOH575 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 D 301 |
| Chain | Residue |
| B | ASN99 |
| B | LYS247 |
| D | HIS98 |
| D | ILE243 |
| D | PRO244 |
| D | LYS247 |
| D | HOH425 |
| D | HOH436 |
| D | HOH523 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 302 |
| Chain | Residue |
| D | HIS231 |
| D | LEU232 |
| D | GLN233 |
| D | HOH446 |
| D | HOH550 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT D 303 |
| Chain | Residue |
| D | ASP80 |
| D | ASP81 |
| D | HIS131 |
| D | HIS135 |
| D | PXU171 |
| D | TYR172 |
| D | HIS225 |
| D | HOH557 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01014 |
| Chain | Residue | Details |
| A | ASP80 | |
| B | ASP80 | |
| C | ASP80 | |
| D | ASP80 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01014 |
| Chain | Residue | Details |
| A | HIS225 | |
| B | HIS225 | |
| C | HIS225 | |
| D | HIS225 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|Ref.6 |
| Chain | Residue | Details |
| A | ASP81 | |
| D | ASP81 | |
| D | HIS131 | |
| D | HIS135 | |
| A | HIS131 | |
| A | HIS135 | |
| B | ASP81 | |
| B | HIS131 | |
| B | HIS135 | |
| C | ASP81 | |
| C | HIS131 | |
| C | HIS135 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: 2-hydroxyproline; partial => ECO:0000269|PubMed:28333455 |
| Chain | Residue | Details |
| A | PXU171 | |
| B | PXU171 | |
| C | PXU171 | |
| D | PXU171 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 996 |
| Chain | Residue | Details |
| C | ASP80 | proton acceptor |
| C | ASP81 | metal ligand |
| C | HIS131 | metal ligand |
| C | HIS135 | metal ligand |
| C | PXU171 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | HIS225 | proton donor |
