Structure of PDB 4iy7 Chain B

Receptor sequence
>4iy7B (length=381) Species: 291331 (Xanthomonas oryzae pv. oryzae KACC 10331) [Search protein sequence]
ALSLATLAIHGGQSPDPSTGAVMPPIYATSTYAQSSPGEHQGFEYSRTHN
PTRFAYERCVAALEGGTRAFAFASGMAATSTVMELLDAGSHVVAMDDLYG
GTFRLFERVRRRTAGLDFSFVDLTDPAAFKAAIRADTKMVWIETPTNPML
KLVDIAAIAVIARKHGLLTVVDNTFASPMLQRPLSLGADLVVHSATKYLN
GHSDMVGGIAVVGDNAELAEQMAFLQNSIGGVQGPFDSFLALRGLKTLPL
RMRAHCENALALAQWLETHPAIEKVIYPGLASHPQHVLAKRQMSGFGGIV
SIVLKGGFDAAKRFCEKTELFTLAESLGGVESLVNHPAVMTHASIPVARR
EQLGISDALVRLSVGIEDLGDLRGDLERALV
3D structure
PDB4iy7 PLP undergoes conformational changes during the course of an enzymatic reaction.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B Y58 T61 N240 Y45 T48 N227
BS02 0JO B Y58 R60 Y45 R47
BS03 SER B Y112 R117 E338 Y99 R104 E325
BS04 PYR B Q234 F237 Q221 F224
BS05 KOU B G88 M89 Y112 E156 N160 D185 S207 K210 S339 L340 T354 R374 G75 M76 Y99 E143 N147 D172 S194 K197 S326 L327 T341 R361
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4iy7, PDBe:4iy7, PDBj:4iy7
PDBsum4iy7
PubMed24531493
UniProtQ5H4T8

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