3QFH
2.05 Angstrom Resolution Crystal Structure of Epidermin Leader Peptide Processing Serine Protease (EpiP) from Staphylococcus aureus.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008233 | molecular_function | peptidase activity |
C | 0008236 | molecular_function | serine-type peptidase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004252 | molecular_function | serine-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008233 | molecular_function | peptidase activity |
D | 0008236 | molecular_function | serine-type peptidase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0004252 | molecular_function | serine-type endopeptidase activity |
E | 0006508 | biological_process | proteolysis |
E | 0008233 | molecular_function | peptidase activity |
E | 0008236 | molecular_function | serine-type peptidase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0004252 | molecular_function | serine-type endopeptidase activity |
F | 0006508 | biological_process | proteolysis |
F | 0008233 | molecular_function | peptidase activity |
F | 0008236 | molecular_function | serine-type peptidase activity |
F | 0046872 | molecular_function | metal ion binding |
G | 0004252 | molecular_function | serine-type endopeptidase activity |
G | 0006508 | biological_process | proteolysis |
G | 0008233 | molecular_function | peptidase activity |
G | 0008236 | molecular_function | serine-type peptidase activity |
G | 0046872 | molecular_function | metal ion binding |
H | 0004252 | molecular_function | serine-type endopeptidase activity |
H | 0006508 | biological_process | proteolysis |
H | 0008233 | molecular_function | peptidase activity |
H | 0008236 | molecular_function | serine-type peptidase activity |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA A 1 |
Chain | Residue |
A | LYS409 |
A | SO4460 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 4 |
Chain | Residue |
A | MET343 |
A | PRO434 |
A | PHE435 |
A | SER436 |
F | ARG385 |
F | HOH1363 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 5 |
Chain | Residue |
A | PRO416 |
A | ASP417 |
A | HOH1480 |
D | LYS38 |
A | HIS415 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 458 |
Chain | Residue |
A | ASN39 |
A | THR40 |
A | HIS62 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 459 |
Chain | Residue |
A | GLN425 |
A | HIS440 |
A | HOH489 |
F | ARG385 |
F | HOH477 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 460 |
Chain | Residue |
A | NA1 |
A | LYS130 |
A | HIS131 |
A | HIS411 |
A | HOH1537 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 461 |
Chain | Residue |
A | LYS219 |
H | ASN121 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 462 |
Chain | Residue |
A | LYS50 |
A | HIS72 |
A | ALA75 |
A | HOH1111 |
A | HOH1163 |
B | LYS374 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 6 |
Chain | Residue |
B | HIS415 |
B | ASP417 |
H | LYS38 |
H | HOH1447 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 7 |
Chain | Residue |
B | MET343 |
B | PRO434 |
B | PHE435 |
B | SER436 |
B | HOH1377 |
E | ARG385 |
E | HOH1105 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 458 |
Chain | Residue |
B | ASN39 |
B | THR40 |
B | HIS62 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 459 |
Chain | Residue |
B | GLN425 |
B | LYS430 |
B | HIS440 |
E | ARG385 |
E | HOH488 |
E | HOH489 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 460 |
Chain | Residue |
B | LYS130 |
B | HIS131 |
B | HIS411 |
B | HOH924 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 461 |
Chain | Residue |
A | LYS374 |
B | LYS50 |
B | HIS72 |
B | ALA75 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 462 |
Chain | Residue |
B | LEU335 |
B | ARG437 |
B | TYR438 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 463 |
Chain | Residue |
B | ASN152 |
C | LYS49 |
G | LYS365 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 458 |
Chain | Residue |
C | ASN39 |
C | THR40 |
C | HIS62 |
C | HOH700 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 459 |
Chain | Residue |
C | PRO129 |
C | LYS130 |
C | HIS131 |
C | HIS411 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 460 |
Chain | Residue |
A | LYS414 |
C | LYS433 |
C | PRO434 |
C | ARG437 |
C | TYR438 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 461 |
Chain | Residue |
C | ARG385 |
C | HOH495 |
C | HOH1488 |
F | LYS430 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA D 2 |
Chain | Residue |
D | ASN39 |
D | ALA41 |
D | SO4459 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 9 |
Chain | Residue |
B | ARG385 |
D | GLN425 |
D | HIS440 |
D | HOH485 |
D | HOH490 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 10 |
Chain | Residue |
D | GLN331 |
D | LYS332 |
D | TYR357 |
D | LYS374 |
D | HOH516 |
D | HOH1230 |
site_id | CC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 D 458 |
Chain | Residue |
D | PRO129 |
D | LYS130 |
D | HIS131 |
D | HIS411 |
D | HOH1342 |
D | HOH1343 |
D | HOH1344 |
G | LYS145 |
G | ASN146 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 459 |
Chain | Residue |
D | NA2 |
D | ASN39 |
D | THR40 |
D | HIS62 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL E 8 |
Chain | Residue |
B | HIS179 |
E | PRO129 |
E | LYS130 |
E | HIS131 |
site_id | CC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 458 |
Chain | Residue |
E | HIS415 |
E | PRO416 |
E | ASP417 |
E | LYS418 |
site_id | DC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 459 |
Chain | Residue |
B | LYS151 |
E | LYS414 |
E | HIS415 |
site_id | DC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 460 |
Chain | Residue |
E | SER429 |
E | LYS430 |
E | ASN431 |
E | LYS447 |
G | ASN383 |
G | ARG385 |
site_id | DC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 461 |
Chain | Residue |
E | LYS433 |
E | ARG437 |
E | TYR438 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 462 |
Chain | Residue |
E | ASN39 |
E | THR40 |
E | HIS62 |
site_id | DC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 458 |
Chain | Residue |
F | HIS415 |
F | PRO416 |
F | ASP417 |
F | LYS418 |
site_id | DC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 F 459 |
Chain | Residue |
C | ASN383 |
C | ARG385 |
F | THR428 |
F | SER429 |
F | LYS430 |
F | ASN431 |
F | HOH1364 |
site_id | DC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 F 460 |
Chain | Residue |
F | LYS433 |
F | ARG437 |
F | TYR438 |
site_id | DC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 461 |
Chain | Residue |
F | ASN39 |
F | THR40 |
F | HIS62 |
H | GLN299 |
site_id | DC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 G 458 |
Chain | Residue |
B | LYS414 |
G | LYS433 |
G | PRO434 |
G | ARG437 |
G | TYR438 |
site_id | EC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 459 |
Chain | Residue |
G | ASN39 |
G | THR40 |
G | HIS62 |
site_id | EC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 460 |
Chain | Residue |
G | LYS130 |
G | HIS131 |
G | HIS411 |
site_id | EC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 461 |
Chain | Residue |
G | ARG385 |
G | HOH489 |
G | HOH977 |
site_id | EC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA H 3 |
Chain | Residue |
H | ASN39 |
H | THR40 |
H | ALA41 |
H | SO4461 |
site_id | EC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 H 458 |
Chain | Residue |
A | ARG385 |
H | GLN425 |
H | HIS440 |
H | HOH475 |
H | HOH482 |
site_id | EC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 H 459 |
Chain | Residue |
H | GLN331 |
H | LYS332 |
H | TYR357 |
H | LYS374 |
H | HOH467 |
H | HOH1376 |
site_id | EC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 H 460 |
Chain | Residue |
C | ASN146 |
H | LYS130 |
H | HIS131 |
H | HIS411 |
H | HOH1372 |
H | HOH1373 |
site_id | EC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 H 461 |
Chain | Residue |
H | NA3 |
H | ASN39 |
H | THR40 |
H | HIS62 |
H | HOH1419 |
site_id | EC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 H 462 |
Chain | Residue |
H | LYS50 |
H | HIS72 |
H | ALA75 |
H | HOH1448 |
H | HOH1516 |
H | HOH1557 |
site_id | FC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 H 463 |
Chain | Residue |
F | THR40 |
F | ALA41 |
F | ASN44 |
F | HOH1468 |
H | GLN299 |
H | LYS302 |
H | TYR307 |
H | GLN308 |
H | GLY309 |
Functional Information from PROSITE/UniProt
site_id | PS00136 |
Number of Residues | 12 |
Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. IAIIDTGVmknH |
Chain | Residue | Details |
A | ILE136-HIS147 |
site_id | PS00138 |
Number of Residues | 11 |
Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSlAtPkVSG |
Chain | Residue | Details |
A | GLY391-GLY401 |