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- PDB-1pba: THE NMR STRUCTURE OF THE ACTIVATION DOMAIN ISOLATED FROM PORCINE ... -

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Basic information

Entry
Database: PDB / ID: 1pba
TitleTHE NMR STRUCTURE OF THE ACTIVATION DOMAIN ISOLATED FROM PORCINE PROCARBOXYPEPTIDASE B
ComponentsPROCARBOXYPEPTIDASE B
KeywordsHYDROLASE(C-TERMINAL PEPTIDASE)
Function / homology
Function and homology information


carboxypeptidase B / metallocarboxypeptidase activity / cytoplasmic vesicle / proteolysis / extracellular space / zinc ion binding
Similarity search - Function
Metallocarboxypeptidase-like / Carboxypeptidase B, carboxypeptidase domain / Carboxypeptidase, activation peptide / Metallocarboxypeptidase-like, propeptide / Carboxypeptidase activation peptide / Zinc carboxypeptidases, zinc-binding region 2 signature. / Zinc carboxypeptidases, zinc-binding region 1 signature. / Zn_pept / Peptidase family M14 domain profile. / Peptidase M14, carboxypeptidase A ...Metallocarboxypeptidase-like / Carboxypeptidase B, carboxypeptidase domain / Carboxypeptidase, activation peptide / Metallocarboxypeptidase-like, propeptide / Carboxypeptidase activation peptide / Zinc carboxypeptidases, zinc-binding region 2 signature. / Zinc carboxypeptidases, zinc-binding region 1 signature. / Zn_pept / Peptidase family M14 domain profile. / Peptidase M14, carboxypeptidase A / Zinc carboxypeptidase / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesSus scrofa (pig)
MethodSOLUTION NMR
AuthorsVendrell, J. / Wider, G. / Billeter, M. / Aviles, F.X. / Wuthrich, K.
Citation
Journal: EMBO J. / Year: 1991
Title: The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.
Authors: Vendrell, J. / Billeter, M. / Wider, G. / Aviles, F.X. / Wuthrich, K.
#1: Journal: Biochemistry / Year: 1990
Title: Sequence-Specific 1H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B
Authors: Vendrell, J. / Wider, G. / Aviles, F.X. / Wuthrich, K.
History
DepositionNov 18, 1991Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROCARBOXYPEPTIDASE B


Theoretical massNumber of molelcules
Total (without water)9,5181
Polymers9,5181
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: RESIDUE 40 IS A CIS PROLINE.
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein PROCARBOXYPEPTIDASE B


Mass: 9518.359 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sus scrofa (pig) / References: UniProt: P09955, carboxypeptidase B

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR software
NameDeveloperClassification
DIANAGUENTERT,BRAUN,WUTHRICHrefinement
X-PLORBRUNGERrefinement
NMR ensembleConformers submitted total number: 20

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