5CIT: Ran GDP wild type monoclinic crystal form

Ran GDP wild type monoclinic crystal form. Determined by X-ray diffraction at 1.75 Å resolution. Released 9 Sept 2015.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,328
Mol. weight: 49.85 kDa
Ligands: GDP, MG
Released: 9 Sept 2015

Explore 5CIT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CIT contains 24 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: 12 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
β-strand	85-91	7	1
α-helix	95-112	18
β-strand	117-122	6	1
α-helix	133-135	3
α-helix	138-141	4
β-strand	145-148	4	1
β-strand	150	1	3
α-helix	151-153	3
β-strand	155	1	3
α-helix	158-169	12
β-strand	176-178	3	1
α-helix	179-181	3
β-strand	182	1	2
α-helix	183-185	3
α-helix	188-190	3
α-helix	191-204	14

Chain B: 12 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	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	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	133-135	3
β-strand	144-148	5	4
β-strand	150	1	6
α-helix	151-153	3
β-strand	155	1	6
α-helix	158-169	12
β-strand	176-178	3	4
β-strand	182	1	5
α-helix	183-185	3
α-helix	188-190	3
α-helix	191-202	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding nuclear protein Ran	A, B	protein	216	Homo sapiens	P62826 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5CIT_1 GTP-binding nuclear protein Ran (chains A, B)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
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

Catalysis of GTP Hydrolysis by Small GTPases at Atomic Detail by Integration of X-ray Crystallography, Experimental, and Theoretical IR Spectroscopy. Rudack, T., Jenrich, S., Brucker, S. et al. J Biol Chem (2015) 290:24079-24090. DOI 10.1074/jbc.M115.648071 · PubMed

Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3GJ0 1.48 Å, Crystal structure of human RanGDP
7MO5 1.55 Å, Crystal Structure of the ZnF4 of Nucleoporin NUP153 in complex with Ran-GDP
7MO1 1.6 Å, Crystal Structure of the ZnF1 of Nucleoporin NUP153 in complex with Ran-GDP
5CIQ 1.65 Å, Ran GDP wild type tetragonal crystal form
7MO2 1.65 Å, Crystal Structure of the ZnF2 of Nucleoporin NUP153 in complex with Ran-GDP
5CIW 1.75 Å, Ran GDP Y39A mutant monoclinic crystal form
5CJ2 1.75 Å, Ran GDP Y39A mutant triclinic crystal form
1I2M 1.76 Å, Ran-RCC1-SO4 complex
4HAT 1.78 Å, Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1-Ran-RanBP1
3GJ3 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF2 complex
3GJ5 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF4 complex
4HB2 1.8 Å, Crystal structure of CRM1-Ran-RanBP1

Browse structure collections

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