6GMA: FIP200 C-terminal region

Crystal structure of the FIP200 C-terminal region. Determined by X-ray diffraction at 3.2 Å resolution. Released 6 Mar 2019.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 6
Atoms: 5,952
Mol. weight: 96.46 kDa
Released: 6 Mar 2019

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

Secondary structure: helices and β-sheets

6GMA contains 25 α-helices and 37 β-strands across 6 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
α-helix	1456-1486	31
β-strand	1495-1496	2	1
β-strand	1506-1512	7	2
β-strand	1517-1520	4	2
β-strand	1528-1530	3	2
α-helix	1531	1
α-helix	1536-1538	3
β-strand	1554-1566	13	2
α-helix	1576-1577	2
β-strand	1581-1589	9	2

Chain B: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	1456-1485	30
α-helix	1495	1
β-strand	1496-1497	2	1
β-strand	1506-1511	6	3
β-strand	1518-1520	3	3
β-strand	1528-1530	3	3
α-helix	1531	1
α-helix	1534-1537	4
β-strand	1554-1566	13	3
α-helix	1576-1577	2
β-strand	1581-1589	9	3

Chain C: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	1456-1485	30
β-strand	1495-1496	2	4
β-strand	1506-1511	6	5
β-strand	1518-1520	3	5
β-strand	1528-1530	3	5
α-helix	1531	1
α-helix	1534-1537	4
β-strand	1554-1566	13	5
α-helix	1576-1577	2
β-strand	1581-1589	9	5

Chain D: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	1456-1489	34
β-strand	1496-1497	2	4
β-strand	1506-1511	6	6
β-strand	1518-1520	3	6
β-strand	1528-1530	3	6
α-helix	1531	1
α-helix	1536-1538	3
β-strand	1554-1566	13	6
α-helix	1576-1577	2
β-strand	1581-1589	9	6
β-strand	1592	1	7

Chain E: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	1456-1485	30
β-strand	1496-1497	2	7
β-strand	1506-1511	6	7
β-strand	1518-1520	3	7
β-strand	1528-1530	3	7
α-helix	1531	1
α-helix	1536-1538	3
β-strand	1554-1566	13	7
α-helix	1576-1577	2
β-strand	1581-1589	9	7

Chain F: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	1457-1484	28
β-strand	1495-1496	2	7
β-strand	1506-1511	6	8
β-strand	1518-1520	3	8
β-strand	1528-1530	3	8
α-helix	1531	1
α-helix	1534-1537	4
β-strand	1554-1566	13	8
α-helix	1576-1577	2
β-strand	1581-1588	8	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RB1-inducible coiled-coil protein 1	A, B, C, D, E, F	protein	140	Homo sapiens	Q8TDY2 (AlphaFold model)

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

>6GMA_1 RB1-inducible coiled-coil protein 1 (chains A, B, C, D, E, F)
GAARIMLLERTLQLKEEENKRLNQRLMSQSMSSVSSRHSEKIAIRDFQVGDLVLIILDER
HDNYVLFTVSPTLYFLHSESLPALDLKPGEGASGASRRPWVLGKVMEKEYCQAKKAQNRF
KVPLGTKFYRVKAVSWNKKV

Primary citation

FIP200 Claw Domain Binding to p62 Promotes Autophagosome Formation at Ubiquitin Condensates. Turco, E., Witt, M., Abert, C. et al. Mol Cell (2019) 74:330-346.e11. DOI 10.1016/j.molcel.2019.01.035 · 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
7CZG 1.8 Å, Crystal structure of FIP200 Claw domain apo form
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…

Browse structure collections

About this viewer

MolViewer shows 6GMA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.