1I2M: Ran-RCC1-SO4 complex

Ran-RCC1-SO4 complex. Determined by X-ray diffraction at 1.76 Å resolution. Released 2 May 2001.

Method: X-ray diffraction
Resolution: 1.76 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,984
Mol. weight: 134.94 kDa
Released: 2 May 2001

Explore 1I2M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I2M contains 30 α-helices and 91 β-strands across 4 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: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	9-17	9	1
α-helix	23-28	6
β-strand	39-42	4	1
β-strand	45-52	8	1
β-strand	54	1	2
β-strand	59-65	7	1
α-helix	69-72	4
α-helix	76-79	4
β-strand	85-91	7	1
α-helix	95-98	4
α-helix	101-112	12
β-strand	117-122	6	1
α-helix	136-139	4
β-strand	145-149	5	1
β-strand	150	1	3
β-strand	155	1	3
α-helix	159-169	11
β-strand	176	1	2

Chain B: 8 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	35	1	4
β-strand	36-42	7	5
β-strand	56-63	8	5
α-helix	64	1
β-strand	69-74	6	4
β-strand	78-83	6	4
β-strand	88-92	5	4
α-helix	108-110	3
β-strand	113-114	2	4
β-strand	121-126	6	6
β-strand	130-135	6	6
β-strand	140-144	5	6
β-strand	146-148	3	7
β-strand	151-154	4	7
β-strand	157	1	8
β-strand	158	1	7
β-strand	160	1	8
β-strand	162-168	7	6
β-strand	174-179	6	9
β-strand	183-188	6	9
β-strand	193-197	5	9
α-helix	209-211	3
α-helix	216-218	3
α-helix	221-224	4
β-strand	227-228	2	9
β-strand	242-247	6	10
β-strand	251-256	6	10
β-strand	261-266	6	10
β-strand	279-285	7	10
α-helix	287-289	3
β-strand	296-301	6	11
β-strand	305-310	6	11
β-strand	315-319	5	11
α-helix	322-324	3
β-strand	335-340	6	11
β-strand	347-352	6	12
β-strand	356-361	6	12
β-strand	366-370	5	12
β-strand	385-390	6	12
α-helix	394-396	3
β-strand	400-406	7	5
β-strand	410-416	7	5

Chain C: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	9-17	9	13
α-helix	23-28	6
α-helix	45-47	3
β-strand	48-52	5	13
β-strand	54	1	14
β-strand	55	1	15
β-strand	57	1	15
β-strand	59-65	7	13
α-helix	69-72	4
α-helix	78-81	4
β-strand	85-91	7	13
α-helix	95-98	4
α-helix	101-111	11
β-strand	117-122	6	13
α-helix	136-140	5
β-strand	145-149	5	13
β-strand	150	1	16
α-helix	152-154	3
β-strand	155	1	16
α-helix	159-169	11
β-strand	176	1	14

Chain D: 6 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	35	1	17
β-strand	36-42	7	18
β-strand	56-62	7	18
α-helix	63-64	2
β-strand	69-74	6	17
β-strand	78-83	6	17
β-strand	88-92	5	17
α-helix	108-110	3
β-strand	113-114	2	17
β-strand	121-126	6	19
β-strand	130-135	6	19
β-strand	140-144	5	19
β-strand	146-148	3	20
β-strand	151-154	4	20
β-strand	157	1	21
β-strand	158	1	20
β-strand	160	1	21
β-strand	162-167	6	19
β-strand	174-179	6	22
β-strand	183-188	6	22
β-strand	193-197	5	22
α-helix	221-224	4
β-strand	227-228	2	22
β-strand	242-247	6	23
β-strand	251-256	6	23
β-strand	261-265	5	23
β-strand	280-285	6	23
α-helix	287-289	3
β-strand	296-301	6	24
β-strand	305-310	6	24
β-strand	315-319	5	24
α-helix	322-324	3
β-strand	335-340	6	24
β-strand	347-352	6	25
β-strand	356-361	6	25
β-strand	366-370	5	25
β-strand	385-390	6	25
α-helix	394-396	3
β-strand	399-406	8	18
β-strand	410-417	8	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding nuclear protein ran	A, C	protein	216	Homo sapiens	P62826 (AlphaFold model)
Regulator of chromosome condensation 1	B, D	protein	402	Homo sapiens	P18754 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1I2M_1 GTP-BINDING NUCLEAR PROTEIN RAN (chains A, C)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL

Sequence of entity 2 (B, D), FASTA

>1I2M_2 REGULATOR OF CHROMOSOME CONDENSATION 1 (chains B, D)
SKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHT
VCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGR
VFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCG
EQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEG
HVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLG
RAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAVTKDGRVFAWGMGTNYQLGT
GQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQS

Primary citation

Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Renault, L., Kuhlmann, J., Henkel, A. et al. Cell (2001) 105:245-255. DOI 10.1016/S0092-8674(01)00315-4 · 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
5CJ2 1.75 Å, Ran GDP Y39A mutant triclinic crystal form
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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