Structure of PDB 3fqa Chain A

Receptor sequence
>3fqaA (length=426) Species: 269084 (Synechococcus elongatus PCC 6301) [Search protein sequence]
KTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDG
NRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMV
NDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMF
LVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEIA
GVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVITGFRIAYGG
VQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLS
GNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGG
QVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEA
GFTSLAHTEEDIDATLAAARTVMSAL
3D structure
PDB3fqa Absence of a catalytic water confers resistance to the neurotoxin gabaculine.
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V1027 Y1150 D1245 I1248 K1273 A1407
Catalytic site (residue number reindexed from 1) V20 Y143 D238 I241 K266 A400
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 G1123 T1124 Y1150 E1212 N1217 D1245 V1247 I1248 G116 T117 Y143 E205 N210 D238 V240 I241
BS02 GAB A S1029 R1032 W1067 S22 R25 W60 PDBbind-CN: -logKd/Ki=0.49,IC50=320mM
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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Cellular Component
External links
PDB RCSB:3fqa, PDBe:3fqa, PDBj:3fqa
PDBsum3fqa
PubMed19786580
UniProtP24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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