Structure of PDB 1i41 Chain H

Receptor sequence
>1i41H (length=396) Species: 4097 (Nicotiana tabacum) [Search protein sequence]
YASFLNSDGSVAIHAGERLGRGIVTDAITTPVVNTSAYFFNKTSELIDFK
EKRRASFEYGRYGNPTTVVLEEKISALEGAESTLLMASGMCASTVMLLAL
VPAGGHIVTTTDCYRKTRIFIETILPKMGITATVIDPADVGALELALNQK
KVNLFFTESPTNPFLRCVDIELVSKLCHEKGALVCIDGTFATPLNQKALA
LGADLVLHSATKFLGGHNDVLAGCISGPLKLVSEIRNLHHILGGALNPNA
AYLIIRGMKTLHLRVQQQNSTALRMAEILEAHPKVRHVYYPGLQSHPEHH
IAKKQMTGFGGAVSFEVDGDLLTTAKFVDALKIPYIAPSFGGCESIVDQP
AIMSYWDLSQSDRAKYGIMDNLVRFSFGVEDFDDLKADILQALDSI
3D structure
PDB1i41 Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor.
ChainH
Resolution3.2 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 HEN H E107 Y108 R110 Y111 E58 Y59 R61 Y62
BS02 HEN H S137 G138 M139 Y163 E207 D236 S258 K261 F389 R423 S88 G89 M90 Y114 E158 D187 S209 K212 F340 R374
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:1i41, PDBe:1i41, PDBj:1i41
PDBsum1i41
PubMed11518531
UniProtQ9ZPL5

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