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|
eF-site ID
|
1lhl-A |
|
PDB Code
|
1lhl |
|
Chain
|
A |
|
click to enlarge
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Title
|
ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS |
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Classification
|
HYDROLASE(O-GLYCOSYL) |
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Compound
|
HUMAN LYSOZYME |
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Source
|
Homo sapiens (Human) (LYSC_HUMAN) |
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Sequence
|
A: |
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNT
RATNYNPGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLS
CSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD
VRQYVQGCGV
|
|
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Description
|
(1) |
LYSOZYME (E.C.3.2.1.17) MUTANT WITH ALA 47 REPLACED BY PROLINE (A47P)
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Functional site
|
|
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1)
|
chain |
A |
| residue |
35 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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2)
|
chain |
A |
| residue |
53 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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3)
|
chain |
A |
| residue |
77-95 |
| type |
prosite |
| sequence |
CHLSCSALLQDNIADAVAC
|
| description |
GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. ChlsCsaLlqdNIadavaC
|
| source |
prosite : PS00128
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