Structure of PDB 2bwo Chain D

Receptor sequence

>2bwoD (length=397) Species: 1061 (Rhodobacter capsulatus)

MDYNLALDKAIQKLHDEGRYRTFIDIEREKGAFPKAQWNRPDGGKQDITV
WCGNDYLGMGQHPVVLAAMHEALEAVGAGSGGTRNISGTTAYHRRLEAEI
AGLHQKEAALVFSSAYNANDATLSTLRVLFPGLIIYSDSLNHASMIEGIK
RNAGPKRIFRHNDVAHLRELIAADDPAAPKLIAFESVYSMDGDFGPIKEI
CDIAEEFGALTYIDEVHAVGMYGPRGAGVAERDGLMHRIDIFNGTLAKAY
GVFGGYIAASARMVDAVRSYAPGFIFSTSLPPAIAAGAQASIAFLKTAEG
QKLRDAQQMHAKVLKMRLKALGMPIIDHGSHIVPVVIGDPVHTKAVSDML
LSDYGVYVQPINFPTVPRGTERLRFTPSPVHDLKQIDGLVHAMDLLW

3D structure

• PDB: 2bwo Crystal Structure of 5-Aminolevulinate Synthase, the First Enzyme of Heme Biosynthesis, and its Link to Xlsa in Humans.
• Chain: D
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N54 H142 E185 S189 D214 H217 K248
• Catalytic site (residue number reindexed from 1): N54 H142 E185 S189 D214 H217 K248
• 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	D	R21 S137 S139 N141 H142 A143 I146 K150 K156 I158 P364 T365	R21 S137 S139 N141 H142 A143 I146 K150 K156 I158 P364 T365
BS02	PLP	D	S114 A115 Y116 H142 E185 D214 V216 H217 T245 K248	S114 A115 Y116 H142 E185 D214 V216 H217 T245 K248
BS03	SCA	D	T83 I86 F276	T83 I86 F276
BS04	PLP	D	S277 T278	S277 T278

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

External links

• PDB: RCSB:2bwo, PDBe:2bwo, PDBj:2bwo
• PDBsum: 2bwo
• PubMed: 16121195
• UniProt: P18079|HEM1_RHOCB 5-aminolevulinate synthase (Gene Name=hemA)