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Crystal structure of the ARP4-N-ACTIN(ATP-state) heterodimer bound by a nanobody

Analyse Crystal structure of the ARP4-N-ACTIN(ATP-state) heterodimer bound by a nanobody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NBM
Type: protein
Length: 1,803 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P80428, P60010
Ligands: ATP, CA

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	—	protein	397	—	P80428
C, D	—	protein	364	—	P60010
E, F	—	protein	124	—	—
G	—	protein	17	—	—
H	—	protein	16	—	—

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D
CA · Calcium ion · metal · 4 copies · chains A, B, C, D

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

Compared structures

5NBM · Crystal structure of the Arp4-N-actin(ATP-state) heterodimer bound by a nanobody · the same entry in another collection · chain H against H, TM-score 1.00
P80428 · AlphaFold monomer V2.0 prediction for actin-related protein 4 (P80428) · a predicted model of the same protein · chain B against A, TM-score 0.99
P60010 · AlphaFold monomer V2.0 prediction for actin (P60010) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 P80428
Every structure of UniProt P60010
Elsewhere: RCSB PDB 5NBM · PDBe 5NBM · UniProt P80428 · UniProt P60010

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