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Crystal structure of human cystathionine gamma lyase

Analyse Crystal structure of human cystathionine gamma lyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NMP
Type: protein
Length: 1,532 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P32929

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	376	—	P32929
B	—	protein	376	—	P32929
C	—	protein	390	—	P32929
D	—	protein	390	—	P32929

Compared structures

2NMP · Crystal structure of human Cystathionine gamma lyase · the same entry in another collection · chain D against D, TM-score 1.00
P32929 · AlphaFold monomer V2.0 prediction for cystathionine gamma-lyase (P32929) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P32929
Elsewhere: RCSB PDB 2NMP · PDBe 2NMP · UniProt P32929

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