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PDBsum entry 4zft

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4zft

 

 

 

 

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Contents
Protein chains
185 a.a.
78 a.a.
Ligands
EDO ×5
Metals
_ZN ×4
Waters ×79
PDB id:
4zft
Name: Hydrolase
Title: Catalytic domain of sst2 f403w mutant bound to ubiquitin
Structure: Amsh-like protease sst2. Chain: a, c. Fragment: unp residues 245-435. Synonym: suppressor of ste12 deletion protein 2. Engineered: yes. Mutation: yes. Polyubiquitin-b. Chain: b, d. Fragment: unp residues 77-152.
Source: Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 284812. Strain: 972 / atcc 24843. Gene: sst2, spac19b12.10. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human.
Resolution:
2.30Å     R-factor:   0.194     R-free:   0.235
Authors: A.N.Bueno
Key ref: A.N.Bueno Structure of the catalytic domain of sst2 mutant f403 to ubiquitin at 2.3 angstroms. To be published, .
Date:
21-Apr-15     Release date:   14-Oct-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9P371  (SST2_SCHPO) -  AMSH-like protease sst2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Seq:
Struc:
435 a.a.
185 a.a.*
Protein chains
Pfam   ArchSchema ?
P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens
Seq:
Struc:
229 a.a.
78 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains A, C: E.C.3.4.19.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chains B, D: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

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