Structure of PDB 3bs8 Chain A

Receptor sequence

>3bs8A (length=430) Species: 1423 (Bacillus subtilis)

MRSYEKSKTAFKEAQKLMPGGVNSPVRAFKSVDMDPIFMERGKGSKIFDI
DGNEYIDYVLSWGPLILGHTNDRVVESLKKVAEYGTSFGAPTEVENELAK
LVIDRVPSVEIVRMVSSGTEATMSALRLARGYTGRNKILKFEGCYHGHGD
SLLIKAGSGVATLGLPDSPGVPEGIAKNTITVPYNDLESVKLAFQQFGED
IAGVIVEPVAGNMGVVPPQEGFLQGLRDITEQYGSLLIFDEVMTGFRVDY
NCAQGYFGVTPDLTCLGKVIGGGLPVGAYGGKAEIMEQIAPSGPIYQAGT
LSGNPLAMTAGLETLKQLTPDSYKNFIKKGDRLEEGISKAAEAHGIPHTF
NRAGSMIGFFFTNEPVINYETAKASDLKLFASYYKGMANEGVFLPPSQFE
GLFLSTAHTDEDIENTIQAAEKVFAEISRR

3D structure

• PDB: 3bs8 Crystal structure of Glutamate1-semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine-5'-phosphate
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V22 Y145 E207 D240 M243 K268 G401
• Catalytic site (residue number reindexed from 1): V22 Y145 E207 D240 M243 K268 G401
• Enzyme Commision number: 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase.

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	PMP	A	G118 T119 Y145 H146 E207 N212 D240 V242 K268	G118 T119 Y145 H146 E207 N212 D240 V242 K268

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0008483 transaminase activity
• GO:0016853 isomerase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0042286 glutamate-1-semialdehyde 2,1-aminomutase activity

Biological Process

• GO:0006779 porphyrin-containing compound biosynthetic process
• GO:0006782 protoporphyrinogen IX biosynthetic process
• GO:0033014 tetrapyrrole biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3bs8, PDBe:3bs8, PDBj:3bs8
• PDBsum: 3bs8
• PubMed: 20946885
• UniProt: P30949|GSA_BACSU Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)