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Crystal structure of human cypa mutant K131A

Analyse Crystal structure of human cypa mutant K131A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ALF
Type
protein
Length
164 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-prolyl cis-trans isomerase a
EC
5.2.1.8
UniProt
P62937
Ligands
MG

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8)protein16414% helix, 33% strandP62937

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A

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

Compared structures

  • 2ALF · crystal structure of human CypA mutant K131A · the same entry in another collection · chain A against A, TM-score 1.00

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