4c3v

Extensive counter-ion interactions with subtilisin in aqueous medium, no Cs soakExtensive counter-ion interactions with subtilisin in aqueous medium, no Cs soak

Structural highlights

4c3v is a 1 chain structure with sequence from Bacillus licheniformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.26Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUBC_BACLI Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).^[1] ^[2]

References

↑ Evans KL, Crowder J, Miller ES. Subtilisins of Bacillus spp. hydrolyze keratin and allow growth on feathers. Can J Microbiol. 2000 Nov;46(11):1004-11. doi: 10.1139/w00-085. PMID:11109488 doi:http://dx.doi.org/10.1139/w00-085
↑ Smith EL, DeLange RJ, Evans WH, Landon M, Markland FS. Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships. J Biol Chem. 1968 May 10;243(9):2184-91. PMID:4967581

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OCA

[1] Evans KL, Crowder J, Miller ES. Subtilisins of Bacillus spp. hydrolyze keratin and allow growth on feathers. Can J Microbiol. 2000 Nov;46(11):1004-11. doi: 10.1139/w00-085. PMID:11109488 doi:http://dx.doi.org/10.1139/w00-085

[2] Smith EL, DeLange RJ, Evans WH, Landon M, Markland FS. Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships. J Biol Chem. 1968 May 10;243(9):2184-91. PMID:4967581

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