MolNFT v1 · #182328 · protein

Crystal structure of the tetramerization element of NUP358/RANBP2 (residues 805-832)

7MNK · E3 sumo-protein ligase RANBP2: “Crystal structure of the tetramerization element of NUP358/RANBP2 (residues 805-832)”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #182328 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7MNK
Type: protein
Length: 120 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 sumo-protein ligase RANBP2
UniProt: P49792
Ligands: SO4

Structure

x-ray diffraction · 1 distinct chain · 93% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	E3 sumo-protein ligase RANBP2	protein	30	93% helix, 0% strand	P49792

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A, B, C, D
EDO · 1,2-ethanediol · additive · 4 copies · chains A, D, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

6 interfaces between chains.

B–C · 795 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 736 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 677 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 655 Å² buried · 4 hydrogen bonds · protein-protein
B–D · 397 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7MNK · Crystal structure of the tetramerization element of NUP358/RanBP2 (residues 805-832) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P49792
Elsewhere: RCSB PDB 7MNK · PDBe 7MNK · UniProt P49792

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