Structure of PDB 2bwo Chain E

Receptor sequence
>2bwoE (length=399) Species: 1061 (Rhodobacter capsulatus) [Search protein sequence]
MDYNLALDKAIQKLHDEGRYRTFIDIEREKGAFPKAQWNRPDGGKQDITV
WCGNDYLGMGQHPVVLAAMHEALEAVGAGSGGTRNISGTTAYHRRLEAEI
AGLHQKEAALVFSSAYNANDATLSTLRVLFPGLIIYSDSLNHASMIEGIK
RNAGPKRIFRHNDVAHLRELIAADDPAAPKLIAFESVYSMDGDFGPIKEI
CDIAEEFGALTYIDEVHAVGMYGPRGAGVAERDGLMHRIDIFNGTLAKAY
GVFGGYIAASARMVDAVRSYAPGFIFSTSLPPAIAAGAQASIAFLKTAEG
QKLRDAQQMHAKVLKMRLKALGMPIIDHGSHIVPVVIGDPVHTKAVSDML
LSDYGVYVQPINFPTVPRGTERLRFTPSPVHDLKQIDGLVHAMDLLWAR
3D structure
PDB2bwo Crystal Structure of 5-Aminolevulinate Synthase, the First Enzyme of Heme Biosynthesis, and its Link to Xlsa in Humans.
ChainE
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S189
Catalytic site (residue number reindexed from 1) S189
Enzyme Commision number 2.3.1.37: 5-aminolevulinate 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 SCA E T83 N85 F276 T83 N85 F276
BS02 SCA E R21 S137 D138 S139 H142 I146 K150 K156 I158 S189 M190 T365 R21 S137 D138 S139 H142 I146 K150 K156 I158 S189 M190 T365
BS03 PLP E A115 Y116 H142 E185 S189 D214 V216 H217 K248 A115 Y116 H142 E185 S189 D214 V216 H217 K248
Gene Ontology
Molecular Function
GO:0003870 5-aminolevulinate synthase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006782 protoporphyrinogen IX biosynthetic process
GO:0006783 heme biosynthetic process
GO:0009058 biosynthetic process
GO:0033014 tetrapyrrole biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2bwo, PDBe:2bwo, PDBj:2bwo
PDBsum2bwo
PubMed16121195
UniProtP18079|HEM1_RHOCB 5-aminolevulinate synthase (Gene Name=hemA)

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