Structure of PDB 6w80 Chain A

Receptor sequence

>6w80A (length=430) Species: 522373 (Stenotrophomonas maltophilia K279a)

AHHHHMNHDQSHALFSRAQQLLPGGVNSPVRAFKSVGGEPFFVERADGAY
LYDVDGNRYIDYVGSWGPMIVGHNHPAVRQAVKKAIDNGLSFGAPCAGEV
TMAETITRLVPSCEMVRMVNSGTEATLSAIRLARGATGRNRIVKFEGCYH
GHGDSFLVKAMLTLGVPTSPGVPAGLSELTLTLPYNDFEAATALFEQQGD
DIAGLIIEPVVGNANCIPPREGYLQHLRALCTKHGALLIFDEVMTGFRVA
LGGAQAHYGITPDLTTFGKIIGGGMPVGAYGGRRELMQQIAPAGPIYQAG
TLSGNPVAMAAGLAMLELVQQPGFHADLAERTARLCAGLEAAAADAGVAV
TTTRVGAMFGLFFTSEKVETYAQATACDIPAFNRFFHAMLEQGVFLAPSA
YEAGFLSSAHDDAVIEATLAAARVAFRAAK

3D structure

• PDB: 6w80 Crystal structure of Glutamate-1-semialdehyde 2,1-aminomutase from Stenotrophomonas maltophilia K279a in complex with PLP
• Chain: A
• Resolution: 1.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V21 Y144 D239 K267
• Catalytic site (residue number reindexed from 1): V26 Y149 D241 K269
• 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	A	S116 G117 T118 Y144 H145 E206 N211 D239 V241 K267	S121 G122 T123 Y149 H150 E208 N213 D241 V243 K269

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:6w80, PDBe:6w80, PDBj:6w80
• PDBsum: 6w80
• UniProt: B2FT35|GSA_STRMK Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)