1QG4: Canine GDP-ran F72Y mutant

Canine GDP-ran F72Y mutant. Determined by X-ray diffraction at 2.5 Å resolution. Released 11 Jun 1999.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Canis lupus familiaris
Chains: 2
Atoms: 3,559
Mol. weight: 49.88 kDa
Ligands: GDP, MG
Released: 11 Jun 1999

Explore 1QG4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1QG4 contains 26 α-helices and 24 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, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
α-helix	23-27	5
β-strand	30	1	2
α-helix	31-35	5
β-strand	38-40	3	1
β-strand	45-54	10	1
β-strand	57-66	10	1
α-helix	69-71	3
α-helix	77-80	4
β-strand	85-91	7	1
α-helix	95-99	5
α-helix	101-112	12
β-strand	117-122	6	1
α-helix	133-136	4
α-helix	137-141	5
β-strand	145-148	4	1
β-strand	150	1	3
α-helix	151-153	3
β-strand	155	1	3
α-helix	159-169	11
β-strand	176-178	3	1
α-helix	179-181	3
β-strand	182	1	2
α-helix	183-185	3
α-helix	191-204	14

Chain B: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	4
α-helix	23-27	5
β-strand	30	1	5
α-helix	31-35	5
β-strand	38-40	3	4
β-strand	45-54	10	4
β-strand	57-66	10	4
α-helix	69-71	3
α-helix	74-76	3
α-helix	77-80	4
β-strand	85-91	7	4
α-helix	95-99	5
α-helix	101-112	12
β-strand	117-122	6	4
α-helix	133-136	4
β-strand	144-149	6	4
β-strand	150	1	6
α-helix	151-153	3
β-strand	155	1	6
α-helix	159-169	11
β-strand	176-178	3	4
α-helix	179-181	3
β-strand	182	1	5
α-helix	183-185	3
α-helix	191-208	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (RAN)	A, B	protein	216	Canis lupus familiaris	P62825 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1QG4_1 PROTEIN (RAN) (chains A, B)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKYGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
MG	Magnesium ion	Mg	2

Primary citation

Engineered mutants in the switch II loop of Ran define the contribution made by key residues to the interaction with nuclear transport factor 2 (NTF2) and the role of this interaction in nuclear protein import. Kent, H.M., Moore, M.S., Quimby, B.B. et al. J Mol Biol (1999) 289:565-577. DOI 10.1006/jmbi.1999.2775 · PubMed

Other PDB entries of the same protein (UniProt P62825 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1WA5 2.0 Å, Structure of the Cse1:Imp-alpha:RanGTP complex
1BYU 2.15 Å, Canine GDP-ran
3RAN 2.15 Å, Canine GDP-ran Q69L mutant
1QG2 2.5 Å, Canine GDP-ran R76E mutant
5BXQ 2.5 Å, Structure of the NTF2:RanGDP complex
2BKU 2.7 Å, Kap95p:RanGTP complex
3W3Z 2.7 Å, Crystal structure of Kap121p bound to RanGTP
3A6P 2.92 Å, Crystal structure of Exportin-5:RanGTP:pre-miRNA complex
5YU6 3.0 Å, Crystal structure of exportin-5:RANGTP complex

Browse structure collections

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