3D6E
Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus licheniformis
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B (A, B) | Beta-glucanase | polymer | 201 | 22753.0 | 2 | UniProt (P27051) Pfam (PF00722) | Bacillus licheniformis | Endo-beta-1,3-1,4 glucanase, 1,3-1,4-beta-D-glucan 4-glucanohydrolase, Lichenase |
2 | C, D (A, B) | CALCIUM ION | non-polymer | 40.1 | 2 | Chemie (CA) | |||
3 | E, F (A, B) | water | water | 18.0 | 137 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 201 (UniProt: P27051)
PDB | External Database | Details |
---|---|---|
- | Ala 50 | deletion |
- | Asp 51 | deletion |
- | Gly 52 | deletion |
- | Tyr 53 | deletion |
- | Ser 54 | deletion |
- | Asn 55 | deletion |
- | Gly 56 | deletion |
- | Asn 57 | deletion |
- | Met 58 | deletion |
- | Phe 59 | deletion |
- | Asn 60 | deletion |
- | Cys 61 | deletion |
- | Thr 62 | deletion |
Ala 22 | Arg 64 | engineered mutation |
Phe 23 | Ala 65 | engineered mutation |
Asp 24 | Asn 66 | engineered mutation |
His 25 | Asn 67 | engineered mutation |
Gly 48 | Cys 90 | engineered mutation |
Gly 50 | Glu 92 | engineered mutation |
Gln 52 | Arg 94 | engineered mutation |
Ala 77 | Ser 119 | engineered mutation |
Tyr 79 | Phe 121 | engineered mutation |
Ser 81 | Tyr 123 | engineered mutation |
Tyr 167 | Met 209 | engineered mutation |
Ser 169 | Asn 211 | engineered mutation |
Ala 172 | Asn 214 | engineered mutation |
Tyr 190 | Ser 232 | SEE REMARK 999 |
Ala 191 | Arg 233 | SEE REMARK 999 |
His 192 | Ser 234 | SEE REMARK 999 |
Tyr 193 | Leu 235 | SEE REMARK 999 |
Asn 194 | His 236 | SEE REMARK 999 |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 45506.1 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 80.2 | |
All* | Total formula weight | 45586.2 |