Structure of PDB 5i92 Chain F

Receptor sequence
>5i92F (length=420) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
MSRSETLFNNAQKHIPGGVNSPVRAFKSVGGTPLFFKHAEGAYVLDEDDK
RYVDYVGSWGPMILGHSHPDVLDAVRRQLDHGLSYGAPTALEVEMADLVC
SMVPSMEMVRMVSSGTEATMSAIRLARGYTGRDSIIKFEGCYHGHSDSLL
VKAGSTFGVPNSPGVPAAFAKHTLTLPFNDIEAVRKTLGEVGKEVACIIV
EPVAGNMNCVPPAPGFLEGLREACDEHGVVLIFDEVMTGFRVALGGAQAY
YGVTPDLSTFGKIIGGGMPVGAFGGKREIMQQISPLGPVYQAGTGNPLAM
AAGLTTLRLISRPGFHDELTAYTTRMLDGLQQRADAAGIPFVTTQAGGMF
GLYFSGADAIVTFEDVMASDVERFKRFFHLMLDGGVYLAPSAFEAGFTSI
AHGDKELEITLNAAEKAFAA
3D structure
PDB5i92 Crystal structure of Glutamate-1-semialdehyde 2,1- aminomutase (GSA) from Pseudomonas aeruginosa
ChainF
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V19 Y142 E204 D237 M240 K265 A400
Catalytic site (residue number reindexed from 1) V19 Y142 E201 D234 M237 K262 A395
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 LEU F A422 F423 A425 A417 F418 A420
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5i92, PDBe:5i92, PDBj:5i92
PDBsum5i92
PubMed
UniProtP48247|GSA_PSEAE Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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