Structure of PDB 3fq8 Chain B

Receptor sequence
>3fq8B (length=427) Species: 269084 (Synechococcus elongatus PCC 6301) [Search protein sequence]
FKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVD
GNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEM
VNDAVPSIEMVRFVNSGTEACMAVLRIMRAYTGRDKIIKFEGCYHGHADM
FLVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEI
AGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVITGFRIAYG
GVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTL
SGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACG
GQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFE
AGFTSLAHTEEDIDATLAAARTVMSAL
3D structure
PDB3fq8 Absence of a catalytic water confers resistance to the neurotoxin gabaculine.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V2027 Y2150 E2212 D2245 I2248 K2273 A2407
Catalytic site (residue number reindexed from 1) V21 Y144 E206 D239 I242 K267 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 B G2304 T2305 G298 T299
BS02 PMP B G2123 T2124 Y2150 E2212 N2217 D2245 V2247 I2248 K2273 G117 T118 Y144 E206 N211 D239 V241 I242 K267
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:0006782 protoporphyrinogen IX biosynthetic process
GO:0015995 chlorophyll 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:3fq8, PDBe:3fq8, PDBj:3fq8
PDBsum3fq8
PubMed19786580
UniProtP24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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