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-Structure paper
Title | Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. |
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Journal, issue, pages | J. Mol. Biol., Vol. 254, Page 720-736, Year 1995 |
Publish date | Sep 6, 1995 (structure data deposition date) |
![]() | Mace, J.E. / Agard, D.A. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2 - 2.3 Å |
Structure data | ![]() PDB-1gba: ![]() PDB-1gbb: ![]() PDB-1gbc: ![]() PDB-1gbd: ![]() PDB-1gbe: ![]() PDB-1gbf: ![]() PDB-1gbh: ![]() PDB-1gbi: ![]() PDB-1gbj: ![]() PDB-1gbk: ![]() PDB-1gbl: ![]() PDB-1gbm: |
Chemicals | ![]() ChemComp-SO4: ![]() ChemComp-HOH: |
Source |
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![]() | HYDROLASE (SERINE PROTEINASE) / ACTIVE-SITE MUTATION / HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX |