5CNX
Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008235 | molecular_function | metalloexopeptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046914 | molecular_function | transition metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008235 | molecular_function | metalloexopeptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046914 | molecular_function | transition metal ion binding |
B | 0070006 | molecular_function | metalloaminopeptidase activity |
C | 0004177 | molecular_function | aminopeptidase activity |
C | 0005515 | molecular_function | protein binding |
C | 0006508 | biological_process | proteolysis |
C | 0008233 | molecular_function | peptidase activity |
C | 0008235 | molecular_function | metalloexopeptidase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046914 | molecular_function | transition metal ion binding |
C | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | ASP223 |
A | HIS292 |
A | THR319 |
A | GLU321 |
A | GLU335 |
A | ZN402 |
A | CAC403 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | THR225 |
A | GLU335 |
A | ZN401 |
A | CAC403 |
A | ASP212 |
A | ASP223 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue CAC A 403 |
Chain | Residue |
A | HIS195 |
A | ASP212 |
A | ASP223 |
A | VAL298 |
A | HIS299 |
A | GLU321 |
A | GLU335 |
A | ZN401 |
A | ZN402 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | ARG24 |
A | THR35 |
A | GLY36 |
A | SER37 |
A | TYR55 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue NA A 405 |
Chain | Residue |
A | GLN109 |
A | LEU112 |
A | ALA114 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | ASP223 |
B | HIS292 |
B | THR319 |
B | GLU321 |
B | GLU335 |
B | ZN402 |
B | CAC403 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue ZN B 402 |
Chain | Residue |
B | ASP212 |
B | ASP223 |
B | THR225 |
B | GLU321 |
B | GLU335 |
B | ZN401 |
B | CAC403 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue CAC B 403 |
Chain | Residue |
B | ASP212 |
B | ASP223 |
B | VAL298 |
B | HIS299 |
B | GLU321 |
B | GLU335 |
B | ZN401 |
B | ZN402 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue ZN C 401 |
Chain | Residue |
C | ASP223 |
C | HIS292 |
C | GLU321 |
C | GLU335 |
C | ZN402 |
C | CAC403 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue ZN C 402 |
Chain | Residue |
C | ASP212 |
C | ASP223 |
C | THR225 |
C | GLU321 |
C | GLU335 |
C | ZN401 |
C | CAC403 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue CAC C 403 |
Chain | Residue |
C | ASP212 |
C | ASP223 |
C | VAL298 |
C | HIS299 |
C | GLU321 |
C | GLU335 |
C | ZN401 |
C | ZN402 |