Structure of PDB 1qgn Chain A

Receptor sequence
>1qgnA (length=398) Species: 4097 (Nicotiana tabacum) [Search protein sequence]
MKYASFLNSDGSVAIHAGERLGRGIVTDAITTPVVNTSAYFFNKTSELID
FKEKRRASFEYGRYGNPTTVVLEEKISALEGAESTLLMASGMCASTVMLL
ALVPAGGHIVTTTDCYRKTRIFIETILPKMGITATVIDPADVGALELALN
QKKVNLFFTESPTNPFLRCVDIELVSKLCHEKGALVCIDGTFATPLNQKA
LALGADLVLHSATKFLGGHNDVLAGCISGPLKLVSEIRNLHHILGGALNP
NAAYLIIRGMKTLHLRVQQQNSTALRMAEILEAHPKVRHVYYPGLQSHPE
HHIAKKQMTGFGGAVSFEVDGDLLTTAKFVDALKIPYIAPSFGGCESIVD
QPAIMSYWDLSQSDRAKYGIMDNLVRFSFGVEDFDDLKADILQALDSI
3D structure
PDB1qgn The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R110 Y163 D236 K261
Catalytic site (residue number reindexed from 1) R63 Y116 D189 K214
Enzyme Commision number 4.2.99.9: Transferred entry: 2.5.1.48.
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 PLP A S137 G138 M139 Y163 D236 S258 T260 K261 F389 S90 G91 M92 Y116 D189 S211 T213 K214 F342
BS02 PLP A Y108 R110 Y61 R63
Gene Ontology
Molecular Function
GO:0003962 cystathionine gamma-synthase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009086 methionine biosynthetic process
GO:0019346 transsulfuration

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Molecular Function
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Biological Process
External links
PDB RCSB:1qgn, PDBe:1qgn, PDBj:1qgn
PDBsum1qgn
PubMed10438597
UniProtQ9ZPL5

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