Structure of PDB 1i48 Chain B

Receptor sequence
>1i48B (length=396) Species: 4097 (Nicotiana tabacum) [Search protein sequence]
YASFLNSDGSVAIHAGERLGRGIVTDAITTPVVNTSAYFFNKTSELIDFK
EKRRASFEYGRYGNPTTVVLEEKISALEGAESTLLMASGMCASTVMLLAL
VPAGGHIVTTTDCYRKTRIFIETILPKMGITATVIDPADVGALELALNQK
KVNLFFTESPTNPFLRCVDIELVSKLCHEKGALVCIDGTFATPLNQKALA
LGADLVLHSATKFLGGHNDVLAGCISGPLKLVSEIRNLHHILGGALNPNA
AYLIIRGMKTLHLRVQQQNSTALRMAEILEAHPKVRHVYYPGLQSHPEHH
IAKKQMTGFGGAVSFEVDGDLLTTAKFVDALKIPYIAPSFGGCESIVDQP
AIMSYWDLSQSDRAKYGIMDNLVRFSFGVEDFDDLKADILQALDSI
3D structure
PDB1i48 Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor.
ChainB
Resolution3.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B S137 G138 M139 Y163 D236 T238 S258 T260 K261 F389 S88 G89 M90 Y114 D187 T189 S209 T211 K212 F340
BS02 CCO B Y163 P387 S388 F389 D397 S403 R423 S425 Y114 P338 S339 F340 D348 S354 R374 S376
BS03 PLP B Y108 R110 Y59 R61
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1i48, PDBe:1i48, PDBj:1i48
PDBsum1i48
PubMed11518531
UniProtQ9ZPL5

[Back to BioLiP]