1HRK Lyase date Dec 21, 2000
title Crystal Structure Of Human Ferrochelatase
authors C.K.Wu, H.A.Dailey, J.P.Rose, A.Burden, V.M.Sellers, B.-C.Wang
compound source
Molecule: Ferrochelatase
Chain: A, B
Fragment: Mature Length
Synonym: Protoheme Ferro-Lyase, Heme Synthetase
Ec: 4.99.1.1
Engineered: Yes
Mutation: Yes
Organism_scientific: Homo Sapiens
Organism_common: Human
Expression_system: Escherichia Coli
Expression_system_common: Bacteria
Expression_system_strain: Jm109
Expression_system_vector_type: Plasmid
Expression_system_plasmid: Phdtf20
symmetry Space Group: P 21 21 21
R_factor 0.202
crystal
cell
length a length b length c angle alpha angle beta angle gamma
93.433 87.569 109.699 90.00 90.00 90.00
method X-Ray Diffractionresolution 2.00 Å
ligand CHD, FESenzyme Ferrochelatase. Ferro-protoporphyrin chelatase. Iron chelatase. Heme synthetase. Heme synthase. Lyase E.C.4.99.1.1
note 1HRK is a representative structure
similarity Belongs to the Ferrochelatase family.
subunit Homodimer.
catalytic activ. Protoporphyrin + fe(2+) = protoheme + 2 h(+).
pathway Protoheme biosynthesis; last step.
subcellular loc. Bound to the mitochondrial inner membrane in eukaryotic cells with its active site on the matrix side of the membrane.
enzyme regulation The 2fe-2s cluster could act as a no sensor. Inhibited by nitric oxide (no).
genes BSU10130, HEMF, HEMH (B. subtilis); FECH (H. sapiens); HEM15, MET8, YBR1461, YBR213W, YOR176W (S. cerevisiae)
function Catalyzes the ferrous insertion into protoporphyrin ix.
Gene
Ontology
chain A: GO:0004325, GO:0005739, GO:0006091, GO:0006779, GO:0006783, GO:0008198, GO:0009416, GO:0016829
chain B: GO:0004325, GO:0005739, GO:0006091, GO:0006779, GO:0006783, GO:0008198, GO:0009416, GO:0016829
disease Protoporphyria,erythropoietic
Protoporphyria,erythropoietic,recessive,with liver failure
Depending on the mutation, it can sometimes be recessive. Epp is an dominantly inherited disease of porphyrin metabolism. Defects in fech are the cause of erythropoietic protoporphyria (epp) [mim. 177000]. The clinical manifestations are photosensitivity and hepatobiliary disease.
Primary referenceThe 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis., Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC, Nat Struct Biol 2001 Feb;8(2):156-60. PMID:11175906
Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (147 Kb) [Save to disk]
  • Biological Unit Coordinates (1hrk.pdb1.gz) 130 Kb
  • LPC: Ligand-Protein Contacts for 1HRK
  • CSU: Contacts of Structural Units for 1HRK
  • Likely Quarternary Molecular Structure file(s) for 1HRK
  • Structure Factors (r1hrksf.ent.Z) 497 Kb
  • Retrieve 1HRK in mmCIF format [Save to disk]
  • View 1HRK in 3D
  • On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure.
  • On AstexViewer, from MSD-EBI (viewer documentation).
  • On RasMol (Install RasMol freeware) Here's help on how to use RasMol.
  • Visual 3D analysis of 1HRK
  • STING, shows the sequence and maps the locations of sequence residues or residue ranges onto the 3D structure.
  • Noncovalent Bond Finder displays the closest contacts to ligand or interface, reports distances, walks over water bridges.
  • GRASS (Graphical Representation and Analysis of Structure Server)
  • Cartoon representation from PDB Cartoon
  • Ramachandran plot from PDBSum
  • Structure-derived information
  • Dipole moment, from Dipole Server at Weizmann Institute
  • Crystal Contacts, from CryCo at Weizmann Institute
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1hrka_, region A [Jmol] [rasmolscript] [script source]
        - Domain d1hrkb_, region B [Jmol] [rasmolscript] [script source]
  • Fold representative 1hrk from FSSP and Dali (Families of Structurally Similar Proteins)
  • Class (fold), Architecture (subfold), Topology, Homologous superfamily: CATH
  • Summaries and structural analyses of PDB data files: PDBSum
  • Identification of Protein Pockets & Cavities at CASTp
  • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1hrk_A] [1hrk_B]
  • SWISS-PROT database: [P22830]
  • Domain organization of [HEMZ_HUMAN] by SWISSPFAM
  • Conserved protein region description, domain view and alignment from family Ferrochelatase (PF00762) of Pfam.
  • Alignments of the sequence of 1HRK with the sequences similar proteins can be viewed for classification [HEMZ_HUMAN] at ProtoMap. Click on "Neighbors List", then on the "See Alignments" button below the list.
  • A sequence distance tree ("phylogenetic tree") can be viewed for 1ACL's classification [HEMZ_HUMAN] at ProtoMap. Click on the Cluster number.
  • Other resources with information on 1HRK
  • InterPro: IPR001015
  • PDBREPORT (protein verification by WHAT_CHECK procedures)
  • MMDB (Entrez's Structure Database)
  • Movements, Movies and Images
  • Images from IMB Jena Image Library of Biological Macromolecules.

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