3VI1
Crystal structure of Pseudomonas aerginosa alkaline protease complexed with Substance P(1-6)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001869 | biological_process | negative regulation of complement activation, lectin pathway |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0010765 | biological_process | positive regulation of sodium ion transport |
| A | 0045959 | biological_process | negative regulation of complement activation, classical pathway |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0001869 | biological_process | negative regulation of complement activation, lectin pathway |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0010765 | biological_process | positive regulation of sodium ion transport |
| B | 0045959 | biological_process | negative regulation of complement activation, classical pathway |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | HIS176 |
| A | HIS180 |
| A | HIS186 |
| C | LYS3 |
| C | PRO4 |
| C | GLN6 |
| C | HOH68 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | THR257 |
| A | ASP285 |
| A | GLY287 |
| A | ASP290 |
| A | ARG253 |
| A | GLY255 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 502 |
| Chain | Residue |
| A | GLY288 |
| A | ASP290 |
| A | THR327 |
| A | GLU329 |
| A | HOH557 |
| A | HOH558 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | GLY334 |
| A | GLY336 |
| A | ASP338 |
| A | GLY351 |
| A | ALA353 |
| A | ASP356 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 504 |
| Chain | Residue |
| A | GLY352 |
| A | GLY354 |
| A | ASP356 |
| A | GLY369 |
| A | ALA371 |
| A | ASP374 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 505 |
| Chain | Residue |
| A | GLY370 |
| A | GLY372 |
| A | ASP374 |
| A | ASP400 |
| A | HOH546 |
| A | HOH611 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 506 |
| Chain | Residue |
| A | ASN343 |
| A | VAL345 |
| A | ASN347 |
| A | GLY360 |
| A | LEU362 |
| A | ASP365 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 507 |
| Chain | Residue |
| A | GLY361 |
| A | GLY363 |
| A | ASP365 |
| A | GLU383 |
| A | ASP390 |
| A | HOH545 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 508 |
| Chain | Residue |
| A | ASP446 |
| A | SER448 |
| A | ASP450 |
| A | HIS452 |
| A | ASP454 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | HIS176 |
| B | HIS180 |
| B | HIS186 |
| D | LYS3 |
| D | PRO4 |
| D | HOH35 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 501 |
| Chain | Residue |
| B | ARG253 |
| B | GLY255 |
| B | THR257 |
| B | ASP285 |
| B | GLY287 |
| B | ASP290 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | GLY288 |
| B | ASP290 |
| B | THR327 |
| B | GLU329 |
| B | HOH495 |
| B | HOH520 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | GLY334 |
| B | GLY336 |
| B | ASP338 |
| B | GLY351 |
| B | ALA353 |
| B | ASP356 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 504 |
| Chain | Residue |
| B | GLY352 |
| B | GLY354 |
| B | ASP356 |
| B | GLY369 |
| B | ALA371 |
| B | ASP374 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 505 |
| Chain | Residue |
| B | GLY370 |
| B | GLY372 |
| B | ASP374 |
| B | ASP400 |
| B | HOH491 |
| B | HOH569 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 506 |
| Chain | Residue |
| B | ASN343 |
| B | VAL345 |
| B | ASN347 |
| B | GLY360 |
| B | LEU362 |
| B | ASP365 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 507 |
| Chain | Residue |
| B | GLU383 |
| B | ASP390 |
| B | HOH493 |
| B | GLY361 |
| B | GLY363 |
| B | ASP365 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 508 |
| Chain | Residue |
| B | ASP446 |
| B | SER448 |
| B | ASP450 |
| B | HIS452 |
| B | ASP454 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLTHEIGHTL |
| Chain | Residue | Details |
| A | THR173-LEU182 |
| site_id | PS00330 |
| Number of Residues | 19 |
| Details | HEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DiLygglGaDqLwGGagaD |
| Chain | Residue | Details |
| A | ASP356-ASP374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLU177 | |
| B | GLU177 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 82 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS176 | |
| A | ASP290 | |
| A | THR327 | |
| A | GLU329 | |
| A | GLY334 | |
| A | GLY336 | |
| A | ASP338 | |
| A | ASN343 | |
| A | VAL345 | |
| A | ASN347 | |
| A | GLY351 | |
| A | HIS180 | |
| A | GLY352 | |
| A | ALA353 | |
| A | GLY354 | |
| A | ASP356 | |
| A | GLY360 | |
| A | GLY361 | |
| A | LEU362 | |
| A | GLY363 | |
| A | ASP365 | |
| A | GLY369 | |
| A | HIS186 | |
| A | GLY370 | |
| A | ALA371 | |
| A | GLY372 | |
| A | ASP374 | |
| A | GLU383 | |
| A | ASP390 | |
| A | ASP400 | |
| A | ASP446 | |
| A | SER448 | |
| A | ASP450 | |
| A | ARG253 | |
| A | HIS452 | |
| A | ASP454 | |
| B | HIS176 | |
| B | HIS180 | |
| B | HIS186 | |
| B | ARG253 | |
| B | GLY255 | |
| B | THR257 | |
| B | ASP285 | |
| B | GLY287 | |
| A | GLY255 | |
| B | GLY288 | |
| B | ASP290 | |
| B | THR327 | |
| B | GLU329 | |
| B | GLY334 | |
| B | GLY336 | |
| B | ASP338 | |
| B | ASN343 | |
| B | VAL345 | |
| B | ASN347 | |
| A | THR257 | |
| B | GLY351 | |
| B | GLY352 | |
| B | ALA353 | |
| B | GLY354 | |
| B | ASP356 | |
| B | GLY360 | |
| B | GLY361 | |
| B | LEU362 | |
| B | GLY363 | |
| B | ASP365 | |
| A | ASP285 | |
| B | GLY369 | |
| B | GLY370 | |
| B | ALA371 | |
| B | GLY372 | |
| B | ASP374 | |
| B | GLU383 | |
| B | ASP390 | |
| B | ASP400 | |
| B | ASP446 | |
| B | SER448 | |
| A | GLY287 | |
| B | ASP450 | |
| B | HIS452 | |
| B | ASP454 | |
| A | GLY288 |
