Structure of PDB 1w1z Chain B

Receptor sequence
>1w1zB (length=319) Species: 1098 (Prosthecochloris vibrioformis) [Search protein sequence]
VHRPRRLRRTAALRNLVQENTLTVNDLVFPLFVMPGTNAVEEVSSMPGSF
RFTIDRAVEECKELYDLGIQGIDLFGIPEQKTEDGSEAYNDNGILQQAIR
AIKKAVPELCIMTDVALDPFTPFGHDGLVKDGIILNDETVEVLQKMAVSH
AEAGADFVSPSDMMDGRIGAIREALDETDHSDVGILSYAAKYASSFYGPF
RDALHSAPQFGDKSTYQMNPANTEEAMKEVELDIVEGADIVMVKPGLAYL
DIVWRTKERFDVPVAIYHVSGEYAMVKAAAAKGWIDEDRVMMESLLCMKR
AGADIIFTYYAKEAAKKLR
3D structure
PDB1w1z The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K200 K253
Catalytic site (residue number reindexed from 1) K191 K244
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 SHF B F84 F209 K253 Y276 V278 S279 Y318 F75 F200 K244 Y267 V269 S270 Y309
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:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:1w1z, PDBe:1w1z, PDBj:1w1z
PDBsum1w1z
PubMed15327955
UniProtQ59334|HEM2_CHLP8 Delta-aminolevulinic acid dehydratase (Gene Name=hemB)

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