Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0007155 | biological_process | cell adhesion |
A | 0030001 | biological_process | metal ion transport |
A | 0046872 | molecular_function | metal ion binding |
B | 0007155 | biological_process | cell adhesion |
B | 0030001 | biological_process | metal ion transport |
B | 0046872 | molecular_function | metal ion binding |
C | 0007155 | biological_process | cell adhesion |
C | 0030001 | biological_process | metal ion transport |
C | 0046872 | molecular_function | metal ion binding |
D | 0007155 | biological_process | cell adhesion |
D | 0030001 | biological_process | metal ion transport |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MN A 401 |
Chain | Residue |
A | HIS77 |
A | HIS102 |
A | HIS147 |
A | HIS213 |
A | HIS235 |
A | HIS286 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue MN A 402 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue MN A 403 |
Chain | Residue |
A | ASN58 |
A | ARG187 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue MN A 404 |
Chain | Residue |
A | ILE212 |
A | SER261 |
A | GLU262 |
A | SER267 |
A | VAL270 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue MN A 405 |
Chain | Residue |
A | GLU238 |
A | PRO239 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue MN A 406 |
Chain | Residue |
A | VAL120 |
A | GLU165 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue MN A 407 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue MN A 408 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue MN A 410 |
Chain | Residue |
A | ASP217 |
A | GLU226 |
A | VAL227 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue MN A 411 |
Chain | Residue |
A | ASP249 |
C | ARG221 |
C | GLY224 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue MN A 412 |
Chain | Residue |
A | THR133 |
A | PRO233 |
C | ALA205 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 413 |
Chain | Residue |
A | HIS77 |
A | HIS213 |
A | GLU262 |
A | PHE265 |
A | HOH505 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue PEG A 414 |
Chain | Residue |
A | TYR53 |
A | PRO68 |
A | TYR292 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue PEG A 415 |
Chain | Residue |
A | ASN200 |
A | LYS201 |
A | ALA202 |
A | ILE312 |
A | GLN313 |
C | THR133 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue MN B 401 |
Chain | Residue |
B | HIS77 |
B | HIS102 |
B | HIS147 |
B | HIS213 |
B | HIS235 |
B | HIS286 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue MN B 402 |
Chain | Residue |
B | SER261 |
B | GLU262 |
B | SER267 |
B | VAL270 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue MN B 404 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | HIS77 |
B | HIS102 |
B | HIS235 |
B | HOH505 |
site_id | AE1 |
Number of Residues | 8 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
B | THR48 |
B | LEU49 |
B | HIS50 |
B | ILE70 |
B | PRO71 |
B | PHE74 |
B | PRO76 |
B | TYR292 |
site_id | AE2 |
Number of Residues | 1 |
Details | binding site for residue EDO B 407 |
site_id | AE3 |
Number of Residues | 1 |
Details | binding site for residue EDO B 408 |
site_id | AE4 |
Number of Residues | 6 |
Details | binding site for residue MN C 401 |
Chain | Residue |
C | HIS77 |
C | HIS102 |
C | HIS147 |
C | HIS213 |
C | HIS235 |
C | HIS286 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue MN C 402 |
Chain | Residue |
C | GLU262 |
C | SER267 |
C | VAL270 |
site_id | AE6 |
Number of Residues | 1 |
Details | binding site for residue MN C 403 |
site_id | AE7 |
Number of Residues | 3 |
Details | binding site for residue MN C 404 |
Chain | Residue |
A | GLN250 |
A | HOH532 |
C | PRO203 |
site_id | AE8 |
Number of Residues | 2 |
Details | binding site for residue MN C 405 |
Chain | Residue |
C | ASN58 |
C | ARG187 |
site_id | AE9 |
Number of Residues | 1 |
Details | binding site for residue MN C 408 |
site_id | AF1 |
Number of Residues | 2 |
Details | binding site for residue MN C 409 |
Chain | Residue |
C | ARG275 |
D | ARG192 |
site_id | AF2 |
Number of Residues | 6 |
Details | binding site for residue MN D 401 |
Chain | Residue |
D | HIS77 |
D | HIS102 |
D | HIS147 |
D | HIS213 |
D | HIS235 |
D | HIS286 |
site_id | AF3 |
Number of Residues | 1 |
Details | binding site for residue MN D 402 |
site_id | AF4 |
Number of Residues | 3 |
Details | binding site for residue EDO D 404 |
Chain | Residue |
D | HIS77 |
D | HIS102 |
D | HIS235 |
site_id | AF5 |
Number of Residues | 4 |
Details | binding site for residue EDO D 405 |
Chain | Residue |
D | GLU314 |
D | LEU281 |
D | TYR282 |
D | ARG310 |
Functional Information from PROSITE/UniProt
site_id | PS00867 |
Number of Residues | 8 |
Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. VIEANAKV |
Chain | Residue | Details |
A | VAL120-VAL127 | |