1H6G: Alpha-catenin M-domain

Name: PDB 1H6G: alpha-catenin M-domain
Published: 2001-08-07
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cell adhesion

alpha-catenin M-domain. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Aug 2001.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 4,196
Mol. weight: 58 kDa
Ligands: CA
Released: 7 Aug 2001

Explore 1H6G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1H6G contains 24 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	378-386	9
α-helix	387-389	3
α-helix	398-409	12
α-helix	413-438	26
α-helix	444-473	30
α-helix	478-506	29
α-helix	509-531	23
α-helix	535-559	25
α-helix	567-577	11
α-helix	578-583	6
α-helix	584-598	15
α-helix	603-605	3
α-helix	608-630	23

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	398-409	12
α-helix	413-439	27
α-helix	444-473	30
α-helix	478-506	29
α-helix	508-531	24
α-helix	535-559	25
α-helix	560-562	3
α-helix	567-578	12
α-helix	579-583	5
α-helix	584-597	14
α-helix	608-629	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-1 catenin	A, B	protein	256	HOMO SAPIENS	P35221 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1H6G_1 ALPHA-1 CATENIN (chains A, B)
DLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANL
ACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVR
VLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVV
TSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASR
LVYDGIRDIRKAVLMI

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2

Water and common crystallization additives (CL, MPD) are not listed.

Primary citation

Crystal Structure of the M-Fragment of Alpha-Catenin: Implications for Modulation of Cell Adhesion. Yang, J., Dokurno, P., Tonks, N.K. et al. EMBO J (2001) 20:3645. DOI 10.1093/EMBOJ/20.14.3645 · PubMed

Other PDB entries of the same protein (UniProt P35221 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6V2O 1.27 Å, HLA-B*57:01 presenting the peptide ASLNLPAVSW
6V2P 1.3 Å, HLA-B*57:03 presenting the peptide ASLNLPAVSW
9BL4 1.75 Å, KIR3DL1*086 in complex with HLA-B*57:03 presenting the AW10 peptide
9BL3 2.0 Å, KIR3DL1*114 in complex with HLA-B*57:03 presenting the AW10 peptide
9BL2 2.1 Å, KIR3DL1*001 in complex with HLA-B*57:03 presenting the AW10 peptide
4EHP 2.66 Å, Crystal Structure of human vinculin head domain (residues 1-252) in complex with…
7UTJ 2.77 Å, Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin
6UPV 3.2 Å, Alpha-E-catenin ABD-F-actin complex
4IGG 3.66 Å, Full-length human alpha-catenin crystal structure

Browse structure collections

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