Structure of PDB 2zsm Chain C

Receptor sequence

>2zsmC (length=419) Species: 56636 (Aeropyrum pernix)

EKSRMLFERTKELFPGGVNSPVRAAVKPYPFYVKRGEGAYLYTVDGARIV
DLVLAYGPLILGHKHPRVLEAVEEALARGWLYGAPGEAEVLLAEKILGYV
KRGGMIRFVNSGTEATMTAIRLARGYTGRDLILKFDGCYHGSHDAVLVAA
GGVPTSAGVPEAVARLTLVTPYNDVEALERVFAEYGDRIAGVIVEPVIAN
AGVIPPRREFLAALQRLSRESGALLILDEVVTGFRLGLEGAQGYFNIEGD
IIVLGKIIGGGFPVGAVAGSREVMSLLTPQGKVFNAGTFNAHPITMAAGL
ATLKALEEEPVYSVSREAAKALEEAASEVLDRTGLPYTINRVESMMQLFI
GVEEVSNAAQARKADKKFYVKLHEEMLRRGVFIAPSNLEAVFTGLPHQGE
ALEIAVEGLRSSLKTVLGS

3D structure

• PDB: 2zsm Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from Aeropyrum pernix
• Chain: C
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V27 Y148 E210 D243 V246 K271 A405
• Catalytic site (residue number reindexed from 1): V18 Y139 E195 D228 V231 K256 A390
• 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	C	G302 T303	G287 T288
BS02	PMP	C	S120 G121 T122 Y148 H149 E210 N215 D243 V245 K271	S111 G112 T113 Y139 H140 E195 N200 D228 V230 K256

Gene Ontology

Molecular Function

• 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:2zsm, PDBe:2zsm, PDBj:2zsm
• PDBsum: 2zsm
• UniProt: Q9Y9I9|GSA_AERPE Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)