7CZG: FIP200 Claw domain apo form

Crystal structure of FIP200 Claw domain apo form. Determined by X-ray diffraction at 1.8 Å resolution. Released 31 Mar 2021.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,418
Mol. weight: 49.87 kDa
Released: 31 Mar 2021

Explore 7CZG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CZG contains 14 α-helices and 24 β-strands across 4 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, 6 β-strands

Element	Residues	Length	Sheet
β-strand	1496-1497	2	1
β-strand	1506-1512	7	1
α-helix	1513-1515	3
β-strand	1517-1520	4	1
β-strand	1528-1530	3	1
α-helix	1531	1
α-helix	1532-1534	3
α-helix	1536-1538	3
β-strand	1554-1566	13	1
β-strand	1581-1589	9	1

Chain B: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	1496	1	2
β-strand	1506-1512	7	2
α-helix	1513-1515	3
β-strand	1517-1520	4	2
β-strand	1528-1530	3	2
α-helix	1531	1
α-helix	1534-1537	4
β-strand	1554-1566	13	2
β-strand	1581-1589	9	2

Chain C: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	1495-1496	2	1
β-strand	1506-1512	7	3
β-strand	1517-1520	4	3
β-strand	1528-1530	3	3
α-helix	1531	1
α-helix	1532-1534	3
α-helix	1536-1538	3
β-strand	1554-1566	13	3
β-strand	1581-1589	9	3

Chain D: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	1496	1	2
β-strand	1506-1512	7	2
α-helix	1513-1515	3
β-strand	1517-1520	4	2
β-strand	1528-1530	3	2
α-helix	1531	1
α-helix	1532-1534	3
α-helix	1536-1538	3
β-strand	1554-1566	13	2
β-strand	1581-1589	9	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RB1-inducible coiled-coil protein 1	A, B, C, D	protein	108	Homo sapiens	Q8TDY2 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>7CZG_1 RB1-inducible coiled-coil protein 1 (chains A, B, C, D)
AEFSRHSEKIAIRDFQVGDLVLIILDERHDNYVLFTVSPTLYFLHSESLPALDLKPGEGA
SGASRRPWVLGKVMEKEYCQAKKAQNRFKVPLGTKFYRVKAVSWNKKV

Primary citation

Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation. Zhou, Z., Liu, J., Fu, T. et al. Nat Commun (2021) 12:1570-1570. DOI 10.1038/s41467-021-21874-1 · PubMed

Other PDB entries of the same protein (UniProt Q8TDY2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7D0E 1.4 Å, Crystal structure of FIP200 Claw/p-CCPG1 FIR2
9D34 1.42 Å, FIP200 C-terminal CLAW domain (resid. 1490-1594) in complex with phosphorylated TNIP1…
8YFL 1.5 Å, crystal structure of FIP200 claw/TNIP1_FIR_pS122pS123
8YFM 1.5 Å, Crystal structure of FIP200 claw/TNIP1_FIR_pS122
6DCE 1.56 Å, X-ray structure of FIP200 claw domain
9J54 1.61 Å, Crystal structure of FIP200 Claw in complex with ATG16L1
9LUA 1.97 Å, Crystal structure of FIP200 Claw domain and SMCR8 FIR motif complex
7CZM 2.0 Å, Crystal structure of FIP200 Claw/p-OPtineurin LIR complex
8YFK 2.0 Å, Crystal structure of FIP200 claw/TNIP1_FIR_pS123
7EA2 2.14 Å, crystal structure of NAP1 FIR in complex with RB1CC1 Claw domain
8YFN 2.3 Å, Crystal structure of FIP200 claw in complex with TNIP1_FIR_pS123 peptide with an…
8W6B 2.39 Å, crystal structure of TAX1BP1 SKICH domain in complex with RB1CC1 coiled-coil domain

Browse structure collections

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