Structure of PDB 3gsb Chain A Binding Site BS01

Receptor Information
>3gsb Chain A (length=427) Species: 1131 (Synechococcus sp.) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVD
GNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEM
VNDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADM
FLVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEI
AGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYG
GVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTL
SGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACG
GQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFE
AGFTSLAHTEEDIDATLAAARTVMSAL
Ligand information
Ligand IDPMP
InChIInChI=1S/C8H13N2O5P/c1-5-8(11)7(2-9)6(3-10-5)4-15-16(12,13)14/h3,11H,2,4,9H2,1H3,(H2,12,13,14)
InChIKeyZMJGSOSNSPKHNH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1CN)C
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN)c1O
FormulaC8 H13 N2 O5 P
Name4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE;
PYRIDOXAMINE-5'-PHOSPHATE
ChEMBLCHEMBL1235353
DrugBankDB02142
ZINCZINC000001532708
PDB chain3gsb Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3gsb Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		S122 G123 T124 Y150 N217 D245 V247 M248 K273
Binding residue
(residue number reindexed from 1)		S116 G117 T118 Y144 N211 D239 V241 M242 K267
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) V27 Y150 E212 D245 M248 K273 A407
Catalytic site (residue number reindexed from 1) V21 Y144 E206 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:3gsb, PDBe:3gsb, PDBj:3gsb
PDBsum3gsb
PubMed9144156
UniProtP24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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