Structure of PDB 1h7r Chain A

Receptor sequence
>1h7rA (length=342) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDN
PDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDP
VGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDG
TINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAH
KTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALE
RDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAA
EKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDEEN
3D structure
PDB1h7r The X-Ray Structure of Yeast 5-Aminolaevulinic Acid Dehydratase Complexed with Substrate and Three Inhibitors
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K210 K263
Catalytic site (residue number reindexed from 1) K210 K263
Enzyme Commision number 4.2.1.24: porphobilinogen synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SHU A D131 S179 K210 Y216 F219 K263 Y287 V289 S290 Y329 D131 S179 K210 Y216 F219 K263 Y287 V289 S290 Y329
BS02 ZN A C133 C135 C143 C133 C135 C143
Gene Ontology
Molecular Function
GO:0004655 porphobilinogen synthase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006782 protoporphyrinogen IX biosynthetic process
GO:0006783 heme biosynthetic process
GO:0033014 tetrapyrrole biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1h7r, PDBe:1h7r, PDBj:1h7r
PDBsum1h7r
PubMed11545591
UniProtP05373|HEM2_YEAST Delta-aminolevulinic acid dehydratase (Gene Name=HEM2)

[Back to BioLiP]