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 |