1jo8 Summary


Structural analysis of the yeast actin binding protein Abp1 SH3 domain

The structure was published by Fazi, B., Cope, M.J., Douangamath, A., et al., Wilmanns, M., Cesareni, G., and Castagnoli, L., in 2002 in a paper entitled "Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.3 Å and deposited in 2001.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of ACTIN BINDING PROTEIN. This molecule has the UniProt identifier P15891 (ABP1_YEAST)search. The sample contained 58 residues which is < 90% of the natural sequence. Out of 58 residues 58 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A ACTIN BINDING PROTEIN P15891 (535-592) (ABP1_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 58 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15891 (535 - 592) ACTIN BINDING PROTEIN Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A SH3-domainsearch SH3 Domainssearch SH3 domainsearch
Chain InterPro annotation
A SH3 domainsearch