MolNFT v1 · #136557 · protein

Crystal structure of CDC7 nes peptide (extended) in complex with CRM1- ran-RANBP1

5UWR: “Crystal structure of CDC7 nes peptide (extended) in complex with CRM1- ran-RANBP1”. X-ray diffraction, 3 ligands (GNP, MG, CL). MolNFT v1 #136557 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5UWR
Type: protein
Length: 1,343 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P62826, P41920, P30822, O00311
Ligands: GNP, MG, CL

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	204	—	P62826
B	—	protein	127	—	P41920
C	—	protein	1000	—	P30822
D	—	protein	12	—	O00311

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · chains C
GOL · Glycerol · additive · 3 copies · chains A, C

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

Compared structures

P41920 · AlphaFold monomer V2.0 prediction for ran-specific GTPase-activating protein 1 (P41920) · a predicted model of the same protein · chain B against A, TM-score 0.95
O00311 · AlphaFold monomer V2.0 prediction for cell division cycle 7-related protein kinase… · a predicted model of the same protein · chain D against A, TM-score 0.75

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 P62826
Every structure of UniProt P41920
Every structure of UniProt P30822
Every structure of UniProt O00311
Elsewhere: RCSB PDB 5UWR · PDBe 5UWR · UniProt P62826 · UniProt P41920 · UniProt P30822 · UniProt O00311

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