6RUE
Wolinella succinogenes L-asparaginase mutant V23Q,K24T with L-Asp
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | L-asparaginase | polymer | 318 | 33688.4 | 1 | UniProt (P50286) Pfam (PF00710) Pfam (PF17763) In PDB | Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) | L-ASNase,L-asparagine amidohydrolase |
2 | B | L-asparaginase | polymer | 314 | 33402.1 | 1 | UniProt (P50286) Pfam (PF00710) Pfam (PF17763) In PDB | Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) | L-ASNase,L-asparagine amidohydrolase |
3 | C | L-asparaginase | polymer | 315 | 33473.2 | 1 | UniProt (P50286) Pfam (PF00710) Pfam (PF17763) In PDB | Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) | L-ASNase,L-asparagine amidohydrolase |
4 | D | L-asparaginase | polymer | 317 | 33617.4 | 1 | UniProt (P50286) Pfam (PF00710) Pfam (PF17763) In PDB | Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) | L-ASNase,L-asparagine amidohydrolase |
5 | A, B, C, D | ASPARTIC ACID | non-polymer | 133.1 | 4 | Chemie (ASP) | |||
6 | water | water | 18.0 | 770 | Chemie (HOH) |
Sequence modifications
A: 3 - 330 (UniProt: P50286)
B: 3 - 330 (UniProt: P50286)
C: 3 - 330 (UniProt: P50286)
D: 3 - 330 (UniProt: P50286)
PDB | External Database | Details |
---|---|---|
- | Gly 19 | deletion |
- | Glu 20 | deletion |
- | Ser 21 | deletion |
- | Ser 22 | deletion |
- | Val 23 | deletion |
- | Lys 24 | deletion |
- | Ser 25 | deletion |
- | Ser 26 | deletion |
- | Tyr 27 | deletion |
- | Ser 28 | deletion |
Pro 121 | Ser 121 | conflict |
PDB | External Database | Details |
---|---|---|
- | Ser 18 | deletion |
- | Gly 19 | deletion |
- | Glu 20 | deletion |
- | Ser 21 | deletion |
- | Ser 22 | deletion |
- | Val 23 | deletion |
- | Lys 24 | deletion |
- | Ser 25 | deletion |
- | Ser 26 | deletion |
- | Tyr 27 | deletion |
- | Ser 28 | deletion |
- | Ala 29 | deletion |
- | Gly 30 | deletion |
- | Ala 31 | deletion |
Pro 121 | Ser 121 | conflict |
PDB | External Database | Details |
---|---|---|
- | Ser 18 | deletion |
- | Gly 19 | deletion |
- | Glu 20 | deletion |
- | Ser 21 | deletion |
- | Ser 22 | deletion |
- | Val 23 | deletion |
- | Lys 24 | deletion |
- | Ser 25 | deletion |
- | Ser 26 | deletion |
- | Tyr 27 | deletion |
- | Ser 28 | deletion |
- | Ala 29 | deletion |
- | Gly 30 | deletion |
Pro 121 | Ser 121 | conflict |
PDB | External Database | Details |
---|---|---|
- | Glu 20 | deletion |
- | Ser 21 | deletion |
- | Ser 22 | deletion |
- | Val 23 | deletion |
- | Lys 24 | deletion |
- | Ser 25 | deletion |
- | Ser 26 | deletion |
- | Tyr 27 | deletion |
- | Ser 28 | deletion |
- | Ala 29 | deletion |
- | Gly 30 | deletion |
Pro 121 | Ser 121 | conflict |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 134181.2 | |
Non-Polymers* | Number of molecules | 4 |
Total formula weight | 532.4 | |
All* | Total formula weight | 134713.6 |