1TZP
MEPA, inactive form without ZN in P21
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000270 | biological_process | peptidoglycan metabolic process |
| A | 0004175 | molecular_function | endopeptidase activity |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000270 | biological_process | peptidoglycan metabolic process |
| B | 0004175 | molecular_function | endopeptidase activity |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 561 |
| Chain | Residue |
| A | GLN205 |
| A | HIS206 |
| A | ARG207 |
| A | ALA208 |
| A | HIS209 |
| A | HOH695 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 562 |
| Chain | Residue |
| B | ALA208 |
| B | HIS209 |
| B | HOH603 |
| B | HOH662 |
| B | HOH718 |
| B | GLN205 |
| B | HIS206 |
| B | ARG207 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 563 |
| Chain | Residue |
| A | ASN179 |
| A | PHE204 |
| A | GLN205 |
| A | ARG207 |
| A | HOH716 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 564 |
| Chain | Residue |
| A | LYS149 |
| B | HIS150 |
| B | VAL151 |
| B | VAL152 |
| B | SER153 |
| B | HOH741 |
| B | HOH805 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 565 |
| Chain | Residue |
| A | LEU136 |
| A | ARG137 |
| A | PRO230 |
| A | SER231 |
| A | HOH641 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 566 |
| Chain | Residue |
| B | SER55 |
| B | GLU56 |
| B | HIS57 |
| B | BU1570 |
| B | HOH670 |
| B | HOH726 |
| B | HOH733 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 567 |
| Chain | Residue |
| B | ARG175 |
| B | ARG201 |
| B | PRO229 |
| B | HOH725 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 568 |
| Chain | Residue |
| A | ARG175 |
| A | ARG201 |
| A | HOH732 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 569 |
| Chain | Residue |
| B | ASN179 |
| B | PHE204 |
| B | GLN205 |
| B | ARG207 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BU1 B 570 |
| Chain | Residue |
| A | HIS150 |
| B | GLU56 |
| B | LYS149 |
| B | PHE243 |
| B | GLU244 |
| B | SO4566 |
Functional Information from PROSITE/UniProt
| site_id | PS00414 |
| Number of Residues | 9 |
| Details | PROFILIN Profilin signature. aTpWQkItQ |
| Chain | Residue | Details |
| A | ALA20-GLN28 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15292190 |
| Chain | Residue | Details |
| A | HIS110 | |
| A | HIS113 | |
| A | ASP120 | |
| B | ASP120 | |
| B | ASP147 | |
| B | HIS150 | |
| B | HIS211 | |
| A | ASP147 | |
| A | HIS150 | |
| A | HIS211 | |
| B | HIS110 | |
| B | HIS113 |
