3NXK
Crystal Structure of Probable Cytoplasmic L-asparaginase from Campylobacter jejuni
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004067 | molecular_function | asparaginase activity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006528 | biological_process | asparagine metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
B | 0004067 | molecular_function | asparaginase activity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006528 | biological_process | asparagine metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
C | 0004067 | molecular_function | asparaginase activity |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0006528 | biological_process | asparagine metabolic process |
C | 0016787 | molecular_function | hydrolase activity |
D | 0004067 | molecular_function | asparaginase activity |
D | 0006520 | biological_process | amino acid metabolic process |
D | 0006528 | biological_process | asparagine metabolic process |
D | 0016787 | molecular_function | hydrolase activity |
E | 0004067 | molecular_function | asparaginase activity |
E | 0006520 | biological_process | amino acid metabolic process |
E | 0006528 | biological_process | asparagine metabolic process |
E | 0016787 | molecular_function | hydrolase activity |
F | 0004067 | molecular_function | asparaginase activity |
F | 0006520 | biological_process | amino acid metabolic process |
F | 0006528 | biological_process | asparagine metabolic process |
F | 0016787 | molecular_function | hydrolase activity |
G | 0004067 | molecular_function | asparaginase activity |
G | 0006520 | biological_process | amino acid metabolic process |
G | 0006528 | biological_process | asparagine metabolic process |
G | 0016787 | molecular_function | hydrolase activity |
H | 0004067 | molecular_function | asparaginase activity |
H | 0006520 | biological_process | amino acid metabolic process |
H | 0006528 | biological_process | asparagine metabolic process |
H | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 341 |
Chain | Residue |
A | GLY15 |
A | THR16 |
A | ASP62 |
A | SER63 |
A | GLY94 |
A | THR95 |
A | ASP96 |
A | HOH873 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 342 |
Chain | Residue |
A | ASP112 |
A | LYS113 |
A | LYS205 |
A | HOH899 |
A | SER111 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY A 343 |
Chain | Residue |
A | THR318 |
A | SER319 |
F | LYS213 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 344 |
Chain | Residue |
A | ASN144 |
A | GLY191 |
A | LYS192 |
A | VAL193 |
A | PHE194 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 341 |
Chain | Residue |
B | GLY15 |
B | THR16 |
B | ASP62 |
B | SER63 |
B | GLY94 |
B | THR95 |
B | ASP96 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 342 |
Chain | Residue |
B | SER111 |
B | ASP112 |
B | LYS113 |
B | LYS205 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 343 |
Chain | Residue |
B | TYR327 |
B | LYS330 |
B | TYR331 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 344 |
Chain | Residue |
B | ILE256 |
B | LYS261 |
B | ASP262 |
B | LYS265 |
B | HOH697 |
C | ASN65 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 345 |
Chain | Residue |
B | GLU292 |
B | LYS322 |
B | GLN325 |
B | GLU326 |
B | LEU329 |
B | HOH365 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 341 |
Chain | Residue |
C | GLY15 |
C | THR16 |
C | ASP62 |
C | SER63 |
C | GLY94 |
C | THR95 |
C | ASP96 |
C | HOH387 |
C | HOH823 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 342 |
Chain | Residue |
C | SER111 |
C | ASP112 |
C | LYS205 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 343 |
Chain | Residue |
C | THR318 |
C | SER319 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY C 344 |
Chain | Residue |
A | TYR196 |
C | LYS201 |
C | CYS284 |
C | GLU300 |
C | ASP301 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 D 341 |
Chain | Residue |
D | GLY15 |
D | THR16 |
D | ASP62 |
D | SER63 |
D | GLY94 |
D | THR95 |
D | ASP96 |
D | HOH358 |
D | HOH800 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 342 |
Chain | Residue |
D | SER111 |
D | ASP112 |
D | HOH1038 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL D 343 |
Chain | Residue |
D | THR318 |
D | SER319 |
D | ASP320 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL D 344 |
Chain | Residue |
D | LYS261 |
D | LYS265 |
D | ASP291 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 E 341 |
Chain | Residue |
E | GLY15 |
E | THR16 |
E | ASP62 |
E | SER63 |
E | GLY94 |
E | THR95 |
E | ASP96 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 342 |
Chain | Residue |
E | SER111 |
E | ASP112 |
E | LYS205 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL E 343 |
Chain | Residue |
E | ILE256 |
E | LYS258 |
E | LYS261 |
E | LYS265 |
H | ASN65 |
site_id | CC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL E 344 |
Chain | Residue |
E | LYS236 |
E | LYS270 |
site_id | CC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL E 332 |
Chain | Residue |
E | ARG122 |
E | SER128 |
E | ASP130 |
E | ASN157 |
E | VAL174 |
E | HOH1028 |
F | ARG122 |
F | SER128 |
F | ALA129 |
F | HOH406 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 F 341 |
Chain | Residue |
F | GLY15 |
F | THR16 |
F | SER63 |
F | GLY94 |
F | THR95 |
F | ASP96 |
F | HOH973 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 342 |
Chain | Residue |
F | SER111 |
F | ASP112 |
F | LYS113 |
F | LYS205 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY F 343 |
Chain | Residue |
A | LYS213 |
F | THR318 |
F | SER319 |
site_id | CC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 G 341 |
Chain | Residue |
G | GLY15 |
G | THR16 |
G | SER63 |
G | GLY94 |
G | THR95 |
G | ASP96 |
G | HOH872 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 342 |
Chain | Residue |
G | SER111 |
G | ASP112 |
G | LYS113 |
site_id | DC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 H 341 |
Chain | Residue |
H | GLY15 |
H | THR16 |
H | ASP62 |
H | SER63 |
H | GLY94 |
H | THR95 |
H | ASP96 |
site_id | DC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 H 342 |
Chain | Residue |
H | SER111 |
H | ASP112 |
H | LYS113 |
H | LYS205 |
Functional Information from PROSITE/UniProt