1FT3: Truncated rhogdi K141A mutant

Crystal structure of truncated rhogdi K141A mutant. Determined by X-ray diffraction at 2.8 Å resolution. Released 2 May 2001.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,183
Mol. weight: 31.82 kDa
Released: 2 May 2001

Explore 1FT3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FT3 contains 5 α-helices and 22 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: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	1
β-strand	87-89	3	1
β-strand	102-105	4	2
β-strand	109-110	2	3
β-strand	111-118	8	1
β-strand	123-134	12	2
β-strand	137-149	13	2
α-helix	155	1
β-strand	156-159	4	1
α-helix	160-162	3
β-strand	163-164	2	3
β-strand	173-182	10	2
β-strand	190-199	10	2

Chain B: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	4
β-strand	87-89	3	4
α-helix	95-99	5
β-strand	101-105	5	5
β-strand	109-110	2	6
β-strand	111-118	8	4
β-strand	123-134	12	5
β-strand	137-149	13	5
α-helix	155	1
β-strand	156-159	4	4
α-helix	160-162	3
β-strand	163-164	2	6
β-strand	173-182	10	5
β-strand	190-199	10	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rho GDP-dissociation inhibitor 1	A, B	protein	139	Homo sapiens	P52565 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1FT3_1 RHO GDP-DISSOCIATION INHIBITOR 1 (chains A, B)
MVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSG
MKYIQHTYRKGVKIDATDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDDD
KTDHLSWEWNLTIKKDWKD

Primary citation

Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI. Longenecker, K.L., Garrard, S.M., Sheffield, P.J. et al. Acta Crystallogr D Biol Crystallogr (2001) 57:679-688. DOI 10.1107/S0907444901003122 · PubMed

Other PDB entries of the same protein (UniProt P52565 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1KMT 1.3 Å, Crystal structure of RhoGDI Glu(154,155)Ala mutant
1QVY 1.6 Å, Crystal structure of RhoGDI K(199,200)R double mutant
2JHX 1.6 Å, Crystal structure of rhogdi E155H, E157H mutant
2JHU 1.65 Å, Crystal structure of rhogdi E154A,E155A mutant
2JHT 1.88 Å, Crystal structure of rhogdi K135T,K138T,K141T mutant
2JHY 1.9 Å, Crystal structure of rhogdi E155H, E157H mutant
2JHS 1.95 Å, Crystal structure of rhogdi K135H,K138H,K141H mutant
1FSO 2.0 Å, Crystal structure of truncated human rhogdi quadruple mutant
2JHV 2.07 Å, Crystal structure of rhogdi E154A,E155A mutant
2JI0 2.1 Å, Crystal structure of rhogdi K138Y, K141Y mutant
2JHZ 2.2 Å, Crystal structure of rhogdi E155S, E157S mutant
2BXW 2.4 Å, Crystal structure of rhogdi Lys(135,138,141)Tyr mutant

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