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Crystal structure of NAP1 fir in complex with RB1CC1 claw domain

Analyse Crystal structure of NAP1 fir in complex with RB1CC1 claw domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EA2
Type: protein
Length: 218 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9H6S1, Q8TDY2

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	107	—	Q9H6S1, Q8TDY2
A	—	protein	111	—	Q9H6S1, Q8TDY2

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
P6G · Hexaethylene glycol · additive · chains B, A
FLC · Citrate anion · additive · chains B, A

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

Compared structures

7EA2 · crystal structure of NAP1 FIR in complex with RB1CC1 Claw domain · the same entry in another collection · chain B against B, TM-score 1.00
Q8TDY2 · AlphaFold monomer V2.0 prediction for RB1-inducible coiled-coil protein 1 (Q8TDY2) · a predicted model of the same protein · chain B against A, TM-score 0.83
Q9H6S1 · AlphaFold monomer V2.0 prediction for 5-azacytidine-induced protein 2 (Q9H6S1) · a predicted model of the same protein · chain B against A, TM-score 0.22

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 Q9H6S1
Every structure of UniProt Q8TDY2
Elsewhere: RCSB PDB 7EA2 · PDBe 7EA2 · UniProt Q9H6S1 · UniProt Q8TDY2

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