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 | 0005829 | cellular_component | cytosol |
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 | 0005829 | cellular_component | cytosol |
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 | ACT_SITE: Proton acceptor; for enolization step => ECO:0000255|HAMAP-Rule:MF_01241 |
Chain | Residue | Details |
A | ASP62 | |
B | ASP62 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: For ring-opening step => ECO:0000255|HAMAP-Rule:MF_01241 |
Chain | Residue | Details |
A | ASN128 | |
A | GLU135 | |
B | ASN128 | |
B | GLU135 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor; for ring-opening step => ECO:0000255|HAMAP-Rule:MF_01241 |
Chain | Residue | Details |
A | HIS130 | |
B | HIS130 |