2QK1: Protein STU2

Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1. Determined by X-ray diffraction at 1.7 Å resolution. Released 2 Oct 2007.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,303
Mol. weight: 28.9 kDa
Released: 2 Oct 2007

Explore 2QK1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2QK1 contains 19 α-helices and 2 β-strands across 1 chain. 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: 19 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	318-321	4
β-strand	322	1	1
α-helix	325-327	3
α-helix	332-336	5
α-helix	341-354	14
α-helix	356-358	3
β-strand	362	1	1
α-helix	370-382	13
α-helix	386-403	18
α-helix	410-422	13
α-helix	423-425	3
α-helix	429-445	17
α-helix	456-465	10
α-helix	471-487	17
α-helix	493-498	6
α-helix	499-503	5
α-helix	504-511	8
α-helix	516-533	18
α-helix	536-538	3
α-helix	539-544	6
α-helix	547-558	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein STU2	A	protein	249	Saccharomyces cerevisiae	P46675 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2QK1_1 Protein STU2 (chains A)
GSHMASMLPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQTKKLKSTSQNYSN
LLGIYGHIIQKDANIQAVALAAQSVELICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSV
IEAIRKALLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECTQLFNASMKEEKDG
YSTLQRYLKDEVVPIVIQIVNDTQPAIRTIGFESFAILIKIFGMNTFVKTLEHLDNLKRK
KIEETVKTL

Primary citation

Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170, and EB1. Slep, K.C., Vale, R.D. Mol Cell (2007) 27:976-991. DOI 10.1016/j.molcel.2007.07.023 · PubMed

Other PDB entries of the same protein (UniProt P46675 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6BL7 2.5 Å, S. cerevisiae stu2 coiled coil domain
7KDF 2.72 Å, Structure of Stu2 Bound to dwarf Ndc80c
4U3J 2.81 Å, TOG2:alpha/beta-tubulin complex
4FFB 2.88 Å, A TOG:alpha/beta-tubulin Complex Structure Reveals Conformation-Based Mechanisms For a…

Browse structure collections

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