Structure of PDB 3k28 Chain C

Receptor sequence

>3k28C (length=422) Species: 261594 (Bacillus anthracis str. 'Ames Ancestor')

MRKFDKSIAAFEEAQDLMPGGVNSPVRAFKSVGMNPLFMERGKGSKVYDI
DGNEYIDYVLSWGPLIHGHANDRVVEALKAVAERGTSFGAPTEIENKLAK
LVIERVPSIEIVRMVNSGTEATMSALRLARGYTGRNKILKFIGCYHGHGD
SLLIKAGSGVDSPGVPEGVAKNTITVAYNDLESVKYAFEQFGDDIACVIV
EPVAGNMGVVPPQPGFLEGLREVTEQNGALLIFDEVMTGFRVAYNCGQGY
YGVTPDLTCLGKVIGGGLPVGAYGGKAEIMRQVAPSGPIYQAGTLSGNPL
AMAAGYETLVQLTPESYVEFERKAEMLEAGLRKAAEKHGIPHHINRAGSM
IGIFFTDEPVINYDAAKSSNLQFFAAYYREMVEQGVFLPPSQFEGLFLST
VHSDADIEATIAAAEIAMSKLK

3D structure

• PDB: 3k28 Crystal Structure of a glutamate-1-semialdehyde aminotransferase from Bacillus anthracis with bound Pyridoxal 5'Phosphate
• Chain: C
• Resolution: 1.95 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 E201 D234 M237 K262 G395
• 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	PLP	C	G118 T119 Y145 H146 E207 D240 V242 M243 K268	G118 T119 Y145 H146 E201 D234 V236 M237 K262
BS02	CA	C	I103 V106 P107 I109	I103 V106 P107 I109
BS03	CA	C	F194 N233	F188 N227

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:3k28, PDBe:3k28, PDBj:3k28
• PDBsum: 3k28
• UniProt: Q81LD0|GSA2_BACAN Glutamate-1-semialdehyde 2,1-aminomutase 2 (Gene Name=hemL2)