2GRR: Human RanGAP1-Ubc9-D127S

Crystal Structure of human RanGAP1-Ubc9-D127S. Determined by X-ray diffraction at 1.3 Å resolution. Released 30 May 2006.

Method: X-ray diffraction
Resolution: 1.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,913
Mol. weight: 36.74 kDa
Released: 30 May 2006

Explore 2GRR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2GRR contains 18 α-helices and 7 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: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
β-strand	25-30	6	1
β-strand	36-46	11	1
α-helix	47-48	2
β-strand	57-63	7	1
α-helix	72-73	2
β-strand	74-77	4	1
β-strand	86	1	2
β-strand	91	1	1
β-strand	92	1	2
α-helix	95-97	3
α-helix	109-121	13
α-helix	131-139	9
α-helix	141-154	14

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	434-439	6
α-helix	443-448	6
α-helix	453-459	7
α-helix	466-477	12
α-helix	484-502	19
α-helix	509-519	11
α-helix	536-545	10
α-helix	553-555	3
α-helix	556-564	9
α-helix	568-571	4
α-helix	574-586	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 I	A	protein	161	Homo sapiens	P63279 (AlphaFold model)
Ran GTPase-activating protein 1	B	protein	170	Homo sapiens	P46060 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2GRR_1 Ubiquitin-conjugating enzyme E2 I (chains A)
GSHMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGL
FKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQ
ELLNEPNIQSPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS

Sequence of entity 2 (B), FASTA

>2GRR_2 Ran GTPase-activating protein 1 (chains B)
STGEPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLKVS
SVFKDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANLYG
PLMALNHMVQQDYFPKALAPLLLAFVTKPNSALESCSFARHSLLQTLYKV

Primary citation

Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. Yunus, A.A., Lima, C.D. Nat Struct Mol Biol (2006) 13:491-499. DOI 10.1038/nsmb1104 · PubMed

Other PDB entries of the same protein (UniProt P63279 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5F6E 1.12 Å, Crystal Structure of human Ubc9 (K48A/K49A/E54A)
5F6Y 1.14 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 2 (mercaptobenzoxazole)
5F6V 1.49 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 1 (biphenol from…
5F6U 1.55 Å, Crystal Structure of Ubc9 (K48A/K49A/E54A) complexed with Fragment 8 (JSS190B146)
5F6D 1.55 Å, Crystal structure of Ubc9 (K48A/K49A/E54A) complexed with Fragment 6
5F6X 1.56 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 2 (mercaptobenzoxazole…
5F6W 1.7 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 1 (biphenol)
2GRO 1.7 Å, Crystal Structure of human RanGAP1-Ubc9-N85Q
2GRQ 1.7 Å, Crystal Structure of human RanGAP1-Ubc9-D127A
9GLR 1.72 Å, Crystal Structure of Human UBC9 C93E
2GRN 1.8 Å, Crystal Structure of human RanGAP1-Ubc9
6SYF 1.9 Å, Human Ubc9 with covalent isopeptide ligand

Browse structure collections

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