MolNFT v1 · #162652 · protein

Cryo-EM structure of the N-terminal dc repeat (ndc) of ndc-ndc chimera (human sequence) bound to 14-protofilament GDP-microtubule

6RFD: “Cryo-EM structure of the N-terminal dc repeat (ndc) of ndc-ndc chimera (human sequence) bound to…”. Electron microscopy, 3 ligands (GTP, GDP, MG). MolNFT v1 #162652 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6RFD
Type: protein
Length: 1,821 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P81947, Q6B856, O43602
Ligands: GTP, GDP, MG

Structure

electron microscopy · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, a	—	protein	432	—	P81947
B, b	—	protein	429	—	Q6B856
N	—	protein	99	—	O43602

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, a
GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B, a, b
MG · Magnesium ion · metal · 2 copies · chains A, a

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

Compared structures

6RFD · Cryo-EM structure of the N-terminal DC repeat (NDC) of NDC-NDC chimera (human sequence)… · the same entry in another collection · chain A against A, TM-score 1.00
O43602 · AlphaFold monomer V2.0 prediction for neuronal migration protein doublecortin (O43602) · a predicted model of the same protein · chain N against A, TM-score 0.89

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 P81947
Every structure of UniProt Q6B856
Every structure of UniProt O43602
Elsewhere: RCSB PDB 6RFD · PDBe 6RFD · UniProt P81947 · UniProt Q6B856 · UniProt O43602

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