2RI0
Crystal Structure of glucosamine 6-phosphate deaminase (NagB) from S. mutans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006040 | biological_process | amino sugar metabolic process |
| A | 0006043 | biological_process | glucosamine catabolic process |
| A | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| A | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0004342 | molecular_function | glucosamine-6-phosphate deaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006040 | biological_process | amino sugar metabolic process |
| B | 0006043 | biological_process | glucosamine catabolic process |
| B | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| B | 0006046 | biological_process | N-acetylglucosamine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 234 |
| Chain | Residue |
| B | ALA99 |
| B | ALA100 |
| B | HOH498 |
| B | HOH589 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 235 |
| Chain | Residue |
| B | LEU94 |
| B | ASN96 |
| B | GLU105 |
| B | TYR108 |
| B | HOH433 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BTB A 234 |
| Chain | Residue |
| A | GLU22 |
| A | GLU23 |
| A | PHE26 |
| A | LYS220 |
| B | GLU22 |
| B | GLU23 |
| B | PHE26 |
| B | LYS220 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BTB B 236 |
| Chain | Residue |
| A | HOH513 |
| B | ASN96 |
| B | GLU105 |
| B | HOH400 |
| B | HOH436 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; for enolization step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"For ring-opening step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; for ring-opening step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
