Structure of PDB 1i43 Chain A

Receptor sequence
>1i43A (length=396) Species: 4097 (Nicotiana tabacum) [Search protein sequence]
YASFLNSDGSVAIHAGERLGRGIVTDAITTPVVNTSAYFFNKTSELIDFK
EKRRASFEYGRYGNPTTVVLEEKISALEGAESTLLMASGMCASTVMLLAL
VPAGGHIVTTTDCYRKTRIFIETILPKMGITATVIDPADVGALELALNQK
KVNLFFTESPTNPFLRCVDIELVSKLCHEKGALVCIDGTFATPLNQKALA
LGADLVLHSATKFLGGHNDVLAGCISGPLKLVSEIRNLHHILGGALNPNA
AYLIIRGMKTLHLRVQQQNSTALRMAEILEAHPKVRHVYYPGLQSHPEHH
IAKKQMTGFGGAVSFEVDGDLLTTAKFVDALKIPYIAPSFGGCESIVDQP
AIMSYWDLSQSDRAKYGIMDNLVRFSFGVEDFDDLKADILQALDSI
3D structure
PDB1i43 Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor.
ChainA
Resolution3.1 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) R61 Y114 D187 K212
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 S88 G89 M90 Y114 D187 S209 T211 K212 F340
BS02 PMC A Y163 K261 P387 S403 R423 Y114 K212 P338 S354 R374 PDBbind-CN: -logKd/Ki=3.70,Ki=200uM
BS03 PLP A Y108 R110 Y59 R61
BS04 PMC A E107 Y111 E58 Y62 PDBbind-CN: -logKd/Ki=3.70,Ki=200uM
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:1i43, PDBe:1i43, PDBj:1i43
PDBsum1i43
PubMed11518531
UniProtQ9ZPL5

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