5CJ2: Ran GDP Y39A mutant triclinic crystal form

Ran GDP Y39A mutant triclinic 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: 8
Atoms: 13,388
Mol. weight: 198.94 kDa
Ligands: PO4, MG, GDP
Released: 9 Sept 2015

Explore 5CJ2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CJ2 contains 103 α-helices and 96 β-strands across 8 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: 14 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	1
α-helix	23-27	5
β-strand	30	1	2
α-helix	31-35	5
β-strand	38-40	3	1
α-helix	41-43	3
β-strand	45-54	10	1
β-strand	57-66	10	1
α-helix	69-72	4
α-helix	74-76	3
α-helix	77-80	4
β-strand	85-91	7	1
α-helix	95-99	5
α-helix	101-111	11
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
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	191-202	12

Chain B: 14 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	4
α-helix	23-27	5
β-strand	30	1	5
α-helix	31-35	5
β-strand	38-40	3	4
α-helix	41-43	3
β-strand	45-54	10	4
β-strand	57-66	10	4
α-helix	69-72	4
α-helix	75-76	2
α-helix	77-80	4
β-strand	85-91	7	4
α-helix	95-99	5
α-helix	101-111	11
β-strand	117-122	6	4
α-helix	133-135	3
α-helix	138-142	5
β-strand	145-148	4	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	191-204	14

Chain C: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	7
α-helix	23-27	5
β-strand	30	1	8
α-helix	31-35	5
β-strand	38-40	3	7
β-strand	45-54	10	7
β-strand	57-65	9	7
α-helix	69-71	3
α-helix	77-80	4
β-strand	85-91	7	7
α-helix	95-99	5
α-helix	101-111	11
β-strand	117-122	6	7
α-helix	133-135	3
α-helix	138-142	5
β-strand	145-148	4	7
β-strand	150	1	9
α-helix	151-153	3
β-strand	155	1	9
α-helix	158-169	12
β-strand	176-178	3	7
α-helix	179-181	3
β-strand	182	1	8
α-helix	183-185	3
α-helix	191-205	15

Chain D: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	10
α-helix	23-28	6
β-strand	30	1	11
α-helix	31-35	5
β-strand	38-40	3	10
β-strand	45-54	10	10
β-strand	57-66	10	10
α-helix	69-72	4
α-helix	75-76	2
α-helix	77-80	4
β-strand	85-91	7	10
α-helix	95-99	5
α-helix	101-111	11
β-strand	117-122	6	10
α-helix	133-135	3
α-helix	138-141	4
β-strand	145-148	4	10
β-strand	150	1	12
α-helix	151-153	3
β-strand	155	1	12
α-helix	158-169	12
β-strand	176-178	3	10
β-strand	182	1	11
α-helix	183-185	3
α-helix	191-203	13

Chain E: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	13
α-helix	23-27	5
β-strand	30	1	14
α-helix	31-35	5
β-strand	38-40	3	13
β-strand	45-54	10	13
β-strand	57-65	9	13
α-helix	69-72	4
α-helix	77-80	4
β-strand	85-91	7	13
α-helix	95-99	5
α-helix	101-112	12
β-strand	117-122	6	13
α-helix	133-135	3
α-helix	138-142	5
β-strand	145-148	4	13
β-strand	150	1	15
α-helix	151-153	3
β-strand	155	1	15
α-helix	158-169	12
β-strand	176-178	3	13
α-helix	179-181	3
β-strand	182	1	14
α-helix	183-185	3
α-helix	191-205	15

Chain F: 11 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	16
α-helix	23-27	5
β-strand	30	1	17
α-helix	31-35	5
β-strand	38-40	3	16
α-helix	41-43	3
β-strand	45-54	10	16
β-strand	57-66	10	16
α-helix	69-71	3
α-helix	77-80	4
β-strand	85-91	7	16
α-helix	95-111	17
β-strand	117-122	6	16
α-helix	138-141	4
β-strand	145-148	4	16
β-strand	150	1	18
α-helix	151-153	3
β-strand	155	1	18
α-helix	158-169	12
β-strand	176-178	3	16
β-strand	182	1	17
α-helix	183-185	3
α-helix	191-203	13

Chain G: 11 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	19
α-helix	23-27	5
β-strand	30	1	20
α-helix	31-35	5
β-strand	38-40	3	19
α-helix	41-43	3
β-strand	45-54	10	19
β-strand	57-66	10	19
α-helix	69-71	3
α-helix	77-80	4
β-strand	85-91	7	19
α-helix	95-111	17
β-strand	117-122	6	19
α-helix	138-142	5
β-strand	145-148	4	19
β-strand	150	1	21
α-helix	151-153	3
β-strand	155	1	21
α-helix	158-169	12
β-strand	176-178	3	19
β-strand	182	1	20
α-helix	183-185	3
α-helix	191-203	13

Chain H: 14 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	22
α-helix	23-27	5
β-strand	30	1	23
α-helix	31-35	5
β-strand	38-40	3	22
α-helix	41-43	3
β-strand	45-54	10	22
β-strand	57-66	10	22
α-helix	69-72	4
α-helix	74-76	3
α-helix	77-80	4
β-strand	85-91	7	22
α-helix	95-99	5
α-helix	101-111	11
β-strand	117-122	6	22
α-helix	133-135	3
α-helix	138-141	4
β-strand	145-148	4	22
β-strand	150	1	24
β-strand	155	1	24
α-helix	158-169	12
β-strand	176-178	3	22
α-helix	179-181	3
β-strand	182	1	23
α-helix	183-185	3
α-helix	191-203	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding nuclear protein Ran	A, B, C, D, E, F, G, H	protein	216	Homo sapiens	P62826 (AlphaFold model)

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

>5CJ2_1 GTP-binding nuclear protein Ran (chains A, B, C, D, E, F, G, H)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKAVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2
MG	Magnesium ion	Mg	12
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	8

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
5CIT 1.75 Å, Ran GDP wild type monoclinic crystal form
5CIW 1.75 Å, Ran GDP Y39A mutant monoclinic 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

About this viewer

MolViewer shows 5CJ2 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.