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Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex with 2',5'-dideoxy-adenosine 3'-triphosphate and mg

Analyse Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CUL
Type: protein
Length: 707 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P30803, P26769, P04896

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	189	—	P30803
B	—	protein	190	—	P26769
C	—	protein	328	—	P04896

Compared structures

1CUL · Complex of gs-alpha with the catalytic domains of mammalian adenylyl cyclase: complex… · the same entry in another collection · chain A against A, TM-score 1.00
P04896 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(S) subunit… · a predicted model of the same protein · chain C against A, TM-score 0.99
P26769 · AlphaFold monomer V2.0 prediction for adenylate cyclase type 2 (P26769) · a predicted model of the same protein · chain B against A, TM-score 0.98
P30803 · AlphaFold monomer V2.0 prediction for adenylate cyclase type 5 (P30803) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P30803
Every structure of UniProt P26769
Every structure of UniProt P04896
Elsewhere: RCSB PDB 1CUL · PDBe 1CUL · UniProt P30803 · UniProt P26769 · UniProt P04896

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