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Structure of HIS15ASP hpr after hydrolysis of ringed species.

Analyse Structure of HIS15ASP hpr after hydrolysis of ringed species. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CM2
Type: protein
Length: 85 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0AA04

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	85	—	P0AA04

Compared structures

1CM2 · Structure of HIS15ASP hpr after hydrolysis of ringed species. · the same entry in another collection · chain A against A, TM-score 1.00
P0AA04 · AlphaFold monomer V2.0 prediction for phosphocarrier protein hpr (P0AA04) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P0AA04
Elsewhere: RCSB PDB 1CM2 · PDBe 1CM2 · UniProt P0AA04

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