› 1crm

X-ray diffraction
2Å resolution

STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES

Released:
DOI: 10.2210/pdb1crm/pdb
PDB entry 1crm coloured by chain, front view.
PDB entry 1crm coloured by chain, side view.
PDB entry 1crm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and Function of Carbonic Anhydrases
Kannan KK
Biomolecular Structure, Conformation, Function and Evolution 1 165- (1981)

Function and Biology Details

Reactions catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Urea = cyanamide + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133680 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 1 Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 28.79 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00915 (Residues: 2-261; Coverage: 100%)
Gene name: CA1
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

3 bound ligands:
Ligand HG 4 x HG
Ligand CL 2 x CL
Ligand H2S 1 x H2S
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 81.85Å b: 75.31Å c: 37.759Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 not available not available
Expression system: Not provided

Quick links

Citations

1 mention without citation

Ridge regression estimated linear probability model predictions of O-glycosylation in proteins with structural and sequence data.
Gana et al. (2019)