Structure of PDB 2epj Chain A

Receptor sequence
>2epjA (length=420) Species: 272557 (Aeropyrum pernix K1) [Search protein sequence]
GEKSRMLFERTKELFPGGVNSPVRAAVKPYPFYVKRGEGAYLYTVDGARI
VDLVLAYGPLILGHKHPRVLEAVEEALARGWLYGAPGEAEVLLAEKILGY
VKRGGMIRFVNSGTEATMTAIRLARGYTGRDLILKFDGCYHGSHDAVLVA
AGGVPTSAGVPEAVARLTLVTPYNDVEALERVFAEYGDRIAGVIVEPVIA
NAGVIPPRREFLAALQRLSRESGALLILDEVVTGFRLGLEGAQGYFNIEG
DIIVLGKIIGGGFPVGAVAGSREVMSLLTPQGKVFNAGTFNAHPITMAAG
LATLKALEEEPVYSVSREAAKALEEAASEVLDRTGLPYTINRVESMMQLF
IGVEEVSNAAQARKADKKFYVKLHEEMLRRGVFIAPSNLEAVFTGLPHQG
EALEIAVEGLRSSLKTVLGS
3D structure
PDB2epj Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from Aeropyrum pernix
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V27 Y148 E210 D243 V246 K271 A405
Catalytic site (residue number reindexed from 1) V19 Y140 E196 D229 V232 K257 A391
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 S120 G121 T122 Y148 H149 E210 N215 D243 V245 K271 S112 G113 T114 Y140 H141 E196 N201 D229 V231 K257
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:2epj, PDBe:2epj, PDBj:2epj
PDBsum2epj
PubMed
UniProtQ9Y9I9|GSA_AERPE Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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