Structure of PDB 3fqa Chain B Binding Site BS02

Receptor Information
>3fqa Chain B (length=426) Species: 269084 (Synechococcus elongatus PCC 6301) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDG
NRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMV
NDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMF
LVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEIA
GVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVITGFRIAYGG
VQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLS
GNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGG
QVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEA
GFTSLAHTEEDIDATLAAARTVMSAL
Ligand information
Ligand IDGAB
InChIInChI=1S/C7H7NO2/c8-6-3-1-2-5(4-6)7(9)10/h1-4H,8H2,(H,9,10)
InChIKeyXFDUHJPVQKIXHO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(cc(c1)N)C(=O)O
CACTVS 3.341Nc1cccc(c1)C(O)=O
ACDLabs 10.04O=C(O)c1cc(N)ccc1
FormulaC7 H7 N O2
Name3-AMINOBENZOIC ACID;
GABACULINE
ChEMBLCHEMBL307782
DrugBankDB02054
ZINCZINC000000388179
PDB chain3fqa Chain A Residue 2000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3fqa Absence of a catalytic water confers resistance to the neurotoxin gabaculine.
Resolution2.35 Å
Binding residue
(original residue number in PDB)		A2303 G2304 T2305
Binding residue
(residue number reindexed from 1)		A296 G297 T298
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=0.49,IC50=320mM
Enzymatic activity
Catalytic site (original residue number in PDB) V2027 Y2150 E2212 D2245 I2248 K2273 A2407
Catalytic site (residue number reindexed from 1) V20 Y143 E205 D238 I241 K266 A400
Enzyme Commision number 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase.
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:3fqa, PDBe:3fqa, PDBj:3fqa
PDBsum3fqa
PubMed19786580
UniProtP24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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