Danish
PDB ID:  pdb_00001jbq
  • STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.6 Å
  • Deposition date: 2001-06-06
Number of assemblies:  3
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others H (PLPStructure of PLPPLP ), J (PLPStructure of PLPPLP )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 43-397 (1-413)
Mutations (UniProt numbering)
Missing residues 194ASN-200PRO
Structural gaps Exists
Uniprot ID P35520 ￫UniprotKB
S-S bonds 272:275
label_asym_ids of heme G
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 43-397 (1-413)
Mutations (UniProt numbering)
Missing residues 194ASN-200PRO
Structural gaps Exists
Uniprot ID P35520 ￫UniprotKB
S-S bonds 272:275
label_asym_ids of heme I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Assembly ID:  2  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others L (PLPStructure of PLPPLP ), N (PLPStructure of PLPPLP )
Each chain information
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 43-397 (1-413)
Mutations (UniProt numbering)
Missing residues 194ASN-200PRO
Structural gaps Exists
Uniprot ID P35520 ￫UniprotKB
S-S bonds 272:275
label_asym_ids of heme K
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 43-397 (1-413)
Mutations (UniProt numbering)
Missing residues 194ASN-200PRO
Structural gaps Exists
Uniprot ID P35520 ￫UniprotKB
S-S bonds 272:275
label_asym_ids of heme M
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Assembly ID:  3  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others P (PLPStructure of PLPPLP ), R (PLPStructure of PLPPLP )
Each chain information
Chain E heme  
auth_asym_id E
Residue indices (Uniprot) 43-399 (1-413)
Mutations (UniProt numbering)
Missing residues 194ASN-200PRO
Structural gaps Exists
Uniprot ID P35520 ￫UniprotKB
S-S bonds 272:275
label_asym_ids of heme O
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain F heme  
auth_asym_id F
Residue indices (Uniprot) 43-397 (1-413)
Mutations (UniProt numbering)
Missing residues 194ASN-200PRO
Structural gaps Exists
Uniprot ID P35520 ￫UniprotKB
S-S bonds 272:275
label_asym_ids of heme Q
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.16 Å