Structure of PDB 4iyo Chain A

Receptor sequence
>4iyoA (length=381) Species: 291331 (Xanthomonas oryzae pv. oryzae KACC 10331) [Search protein sequence]
ALSLATLAIHGGQSPDPSTGAVMPPIYATSTYAQSSPGEHQGFEYSRTHN
PTRFAYERCVAALEGGTRAFAFASGMAATSTVMELLDAGSHVVAMDDLYG
GTFRLFERVRRRTAGLDFSFVDLTDPAAFKAAIRADTKMVWIETPTNPML
KLVDIAAIAVIARKHGLLTVVDNTFASPMLQRPLSLGADLVVHSATKYLN
GHSDMVGGIAVVGDNAELAEQMAFLQNSIGGVQGPFDSFLALRGLKTLPL
RMRAHCENALALAQWLETHPAIEKVIYPGLASHPQHVLAKRQMSGFGGIV
SIVLKGGFDAAKRFCEKTELFTLAESLGGVESLVNHPAVMTHASIPVARR
EQLGISDALVRLSVGIEDLGDLRGDLERALV
3D structure
PDB4iyo PLP undergoes conformational changes during the course of an enzymatic reaction.
ChainA
Resolution1.8 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) R60 Y112 D185 K210
Catalytic site (residue number reindexed from 1) R47 Y99 D172 K197
Enzyme Commision number 4.4.1.1: cystathionine gamma-lyase.
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 SER A Y112 R117 E338 Y99 R104 E325
BS02 0JO A G88 M89 Y112 N160 D185 S207 K210 S339 L340 T354 R374 G75 M76 Y99 N147 D172 S194 K197 S326 L327 T341 R361
BS03 SER A Y58 T61 N240 Y45 T48 N227
Gene Ontology
Molecular Function
GO:0003962 cystathionine gamma-synthase activity
GO:0016846 carbon-sulfur lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0019346 transsulfuration
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4iyo, PDBe:4iyo, PDBj:4iyo
PDBsum4iyo
PubMed24531493
UniProtQ5H4T8

[Back to BioLiP]