6ARH
Crystal structure of Human NAL at a resolution of 1.6 Angstrom
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016833 | molecular_function | oxo-acid-lyase activity |
A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
A | 0042802 | molecular_function | identical protein binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016833 | molecular_function | oxo-acid-lyase activity |
B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
B | 0042802 | molecular_function | identical protein binding |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0016833 | molecular_function | oxo-acid-lyase activity |
C | 0019262 | biological_process | N-acetylneuraminate catabolic process |
C | 0042802 | molecular_function | identical protein binding |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
D | 0016829 | molecular_function | lyase activity |
D | 0016833 | molecular_function | oxo-acid-lyase activity |
D | 0019262 | biological_process | N-acetylneuraminate catabolic process |
D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue ACT A 401 |
Chain | Residue |
A | ALA16 |
A | GLY52 |
A | THR53 |
A | THR54 |
A | TYR145 |
A | LYS175 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ACT A 402 |
Chain | Residue |
A | HOH522 |
A | HOH535 |
D | TRP121 |
A | GLY264 |
A | VAL265 |
A | LEU287 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue ACT B 401 |
Chain | Residue |
B | ALA16 |
B | PHE49 |
B | GLY52 |
B | THR53 |
B | THR54 |
B | TYR145 |
B | LYS175 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue ACT C 401 |
Chain | Residue |
C | ALA16 |
C | GLY52 |
C | THR53 |
C | THR54 |
C | TYR145 |
C | LYS175 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue ACT C 402 |
Chain | Residue |
B | TRP121 |
C | GLY264 |
C | VAL265 |
C | LEU287 |
C | HOH728 |
C | HOH732 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue ACT C 403 |
Chain | Residue |
B | GLY264 |
B | VAL265 |
C | TRP121 |
C | HOH727 |
C | HOH755 |
C | HOH914 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue ACT D 401 |
Chain | Residue |
D | ALA16 |
D | PHE49 |
D | GLY52 |
D | THR53 |
D | THR54 |
D | TYR145 |
D | LYS175 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue ACT D 402 |
Chain | Residue |
A | LEU118 |
A | TRP121 |
A | HOH659 |
D | GLY264 |
D | VAL265 |
D | LEU287 |
D | HOH550 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A6L4 |
Chain | Residue | Details |
A | TYR145 | |
B | TYR145 | |
C | TYR145 | |
D | TYR145 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000250|UniProtKB:P0A6L4 |
Chain | Residue | Details |
A | LYS175 | |
B | LYS175 | |
C | LYS175 | |
D | LYS175 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A6L4 |
Chain | Residue | Details |
A | THR53 | |
B | SER177 | |
B | GLY201 | |
B | ASP203 | |
B | GLU204 | |
B | SER220 | |
C | THR53 | |
C | THR54 | |
C | SER177 | |
C | GLY201 | |
C | ASP203 | |
A | THR54 | |
C | GLU204 | |
C | SER220 | |
D | THR53 | |
D | THR54 | |
D | SER177 | |
D | GLY201 | |
D | ASP203 | |
D | GLU204 | |
D | SER220 | |
A | SER177 | |
A | GLY201 | |
A | ASP203 | |
A | GLU204 | |
A | SER220 | |
B | THR53 | |
B | THR54 |