1VIX
Crystal structure of a putative peptidase T
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006508 | biological_process | proteolysis |
A | 0006518 | biological_process | peptide metabolic process |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043171 | biological_process | peptide catabolic process |
A | 0045148 | molecular_function | tripeptide aminopeptidase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006508 | biological_process | proteolysis |
B | 0006518 | biological_process | peptide metabolic process |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043171 | biological_process | peptide catabolic process |
B | 0045148 | molecular_function | tripeptide aminopeptidase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 419 |
Chain | Residue |
A | HIS78 |
A | ASP140 |
A | GLU173 |
A | GLU174 |
A | ASP196 |
A | ZN420 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 420 |
Chain | Residue |
A | ZN419 |
A | ASP140 |
A | GLU174 |
A | HIS379 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 419 |
Chain | Residue |
B | HIS78 |
B | ASP140 |
B | GLU173 |
B | ASP196 |
B | ZN420 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 420 |
Chain | Residue |
B | ASP140 |
B | GLU174 |
B | HIS379 |
B | ZN419 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 421 |
Chain | Residue |
A | HIS306 |
A | PRO307 |
A | PRO330 |
A | HIS331 |
A | ARG407 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 422 |
Chain | Residue |
A | GLY380 |
A | LYS381 |
A | HIS382 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 423 |
Chain | Residue |
A | LYS216 |
A | ARG272 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 421 |
Chain | Residue |
A | LYS88 |
A | SO4424 |
A | HOH435 |
B | LYS88 |
B | SO4425 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 422 |
Chain | Residue |
B | LYS216 |
B | ARG272 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 424 |
Chain | Residue |
A | LYS88 |
A | SO4425 |
B | LYS88 |
B | SO4421 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 423 |
Chain | Residue |
A | HIS223 |
B | ARG280 |
B | TYR319 |
B | GLY354 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 424 |
Chain | Residue |
B | PRO330 |
B | HIS331 |
B | ARG407 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 425 |
Chain | Residue |
A | ASP15 |
A | GLN17 |
A | LYS88 |
A | HOH471 |
B | SO4421 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 425 |
Chain | Residue |
A | SO4424 |
B | ASP15 |
B | HOH433 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 426 |
Chain | Residue |
A | GLU29 |
A | TRP32 |
A | HIS36 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 426 |
Chain | Residue |
B | TRP32 |
B | HIS36 |
Functional Information from PROSITE/UniProt
site_id | PS00758 |
Number of Residues | 10 |
Details | ARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. IGFISHvDTS |
Chain | Residue | Details |
A | ILE73-SER82 |
site_id | PS00759 |
Number of Residues | 39 |
Details | ARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. GADdKAgiAeiMtalavlqqkkiphgd..IrVAFtpDEEvG |
Chain | Residue | Details |
A | GLY138-GLY176 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | ASP80 | |
B | ASP80 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | GLU173 | |
B | GLU173 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16021622 |
Chain | Residue | Details |
A | HIS78 | |
B | HIS379 | |
A | ASP140 | |
A | GLU174 | |
A | ASP196 | |
A | HIS379 | |
B | HIS78 | |
B | ASP140 | |
B | GLU174 | |
B | ASP196 |