6IXG: Native apo SH3BP5

Crystal structure of native apo SH3BP5 (P41). Determined by X-ray diffraction at 3.8 Å resolution. Released 20 Mar 2019.

Method: X-ray diffraction
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,577
Mol. weight: 52.94 kDa
Released: 20 Mar 2019

Explore 6IXG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6IXG contains 8 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	42-90	49
α-helix	93-145	53
α-helix	151-199	49
α-helix	202-262	61

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	42-90	49
α-helix	93-141	49
α-helix	152-200	49
α-helix	202-261	60

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SH3 domain-binding protein 5	A, B	protein	228	Homo sapiens	O60239 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6IXG_1 SH3 domain-binding protein 5 (chains A, B)
SHVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDS
KPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEM
LNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKY
YVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHEAAASSAM

Primary citation

Structural basis of guanine nucleotide exchange for Rab11 by SH3BP5. Goto-Ito, S., Morooka, N., Yamagata, A. et al. Life Sci Alliance (2019) 2. DOI 10.26508/lsa.201900297 · PubMed

Other PDB entries of the same protein (UniProt O60239 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4H3B 2.08 Å, Crystal Structure of JNK3 in Complex with SAB Peptide
6DJL 3.1 Å, Crystal structure of the Rab11 GEF SH3BP5 bound to nucleotide free Rab11A
6IXE 3.35 Å, Crystal structure of SeMet apo SH3BP5 (I41)
6IXF 3.6 Å, Crystal structure of SeMet apo SH3BP5 (P41)
6IXV 3.8 Å, Crystal structure of SH3BP5-Rab11a

Browse structure collections

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