Structure of PDB 2e7u Chain A

Receptor sequence

>2e7uA (length=424) Species: 300852 (Thermus thermophilus HB8)

MERPISEAYFQEAKRHIPGGVSSPVRAFKAVGGTPPFLVRGEGAYVWDAD
GNRYLDYVMSWGPLILGHAHPKVLARVRETLERGLTFGAPSPLEVALAKK
VKRAYPFVDLVRFVNSGTEATMSALRLARGYTGRPYIVKFRGNYHGHADG
LLVEAGSGALTLGVPSSAGVPEEYAKLTLVLEYNDPEGLREVLKRRGEEI
AAIIFEPVVGNAGVLVPTEDFLKALHEAKAYGVLLIADEVMTGFRLAFGG
ATELLGLKPDLVTLGKILGGGLPAAAYAGRREIMEKVAPLGPVYQAGTLS
GNPLAMAAGLATLELLEENPGYYAYLEDLGARLEAGLKEVLKEKGLPHTV
NRVGSMITVFFTEGPVVTFQDARRTDTELFKRFFHGLLDRGIYWPPSNFE
AAFLSVAHREEDVEKTLEALRKAL

3D structure

• PDB: 2e7u Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from Thermus thermophilus HB8
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V21 Y144 E206 D238 M241 K266 A401
• Catalytic site (residue number reindexed from 1): V21 Y144 E206 D238 M241 K266 A401
• 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	G117 T118 Y144 H145 N211 D238 V240	G117 T118 Y144 H145 N211 D238 V240

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:2e7u, PDBe:2e7u, PDBj:2e7u
• PDBsum: 2e7u
• UniProt: Q5SJS4|GSA_THET8 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)