Structure of PDB 3fq7 Chain A Binding Site BS01

Receptor Information
>3fq7 Chain A (length=427) Species: 269084 (Synechococcus elongatus PCC 6301) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVD
GNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEM
VNDAVPSIEMVRFVNSGTEACMAVLRIMRAYTGRDKIIKFEGCYHGHADM
FLVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEI
AGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYG
GVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTL
SGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACG
GQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFE
AGFTSLAHTEEDIDATLAAARTVMSAL
Ligand information
Ligand IDPXG
InChIInChI=1S/C15H17N2O7P/c1-9-14(18)13(11(6-16-9)8-24-25(21,22)23)7-17-12-4-2-3-10(5-12)15(19)20/h2-6,17-18H,7-8H2,1H3,(H,19,20)(H2,21,22,23)
InChIKeyWSOQXCGRIUHULI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)c1cc(ccc1)NCc2c(cnc(c2O)C)COP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cccc(c2)C(=O)O)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CNc2cccc(c2)C(O)=O)c1O
FormulaC15 H17 N2 O7 P
Name3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID
ChEMBL
DrugBank
ZINC
PDB chain3fq7 Chain A Residue 1434 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3fq7 Absence of a catalytic water confers resistance to the neurotoxin gabaculine.
Resolution2.15 Å
Binding residue
(original residue number in PDB)		S1029 V1031 W1067 G1123 T1124 Y1150 H1151 E1212 N1217 D1245 V1247 M1248 K1273 E1406
Binding residue
(residue number reindexed from 1)		S23 V25 W61 G117 T118 Y144 H145 E206 N211 D239 V241 M242 K267 E400
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=2.52,IC50=3mM
Enzymatic activity
Catalytic site (original residue number in PDB) V1027 Y1150 D1245 M1248 K1273 A1407
Catalytic site (residue number reindexed from 1) V21 Y144 D239 M242 K267 A401
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:3fq7, PDBe:3fq7, PDBj:3fq7
PDBsum3fq7
PubMed19786580
UniProtP24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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