Structure of PDB 4ywv Chain A

Receptor sequence
>4ywvA (length=455) Species: 1010840 (Streptococcus pyogenes MGAS1882) [Search protein sequence]
AYQTIYPYTNEVLHTFDNMTDQGLADVLERAHLLYKKWRKEDHLEERKAQ
LHQVANILRRDRDKYAEIMTKDMGKLFTEAQGEVDLCADIADYYADKADE
FLMSTPLETDSGQAYYLKQSTGVILAVEPWNFPYYQIMRVFAPNFIVGNP
MVLKHASICPRSAQSFEELVLEAGAEAGSITNLFISYDQVSQVIADKRVV
GVCLTGSERGGASIAEEAGKNLKKTTLELGGDDAFIILDDADWDQLEKVL
YFSRLYNAGQVCTSSKRFIVLDKDYDRFKELLTKVFKTAKWGDPMDPETT
LAPLSSAQAKADVLDQIKLALDHGAELVYGGEAIDHPGHFVMPTIIAGLT
KDNPIYYQEIFGPVGEIYKVSSEEEAIEVANDSNYGLGGTIFSSNQEHAK
AVAAKIETGMSFINSGWTSLPELPFGGIKHSGYGRELSELGFTSFVNEHL
IYIPN
3D structure
PDB4ywv Structural insight into the substrate inhibition mechanism of NADP(+)-dependent succinic semialdehyde dehydrogenase from Streptococcus pyogenes.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N132 K155 E229 C263 E360 E437
Catalytic site (residue number reindexed from 1) N131 K154 E228 C262 E359 E436
Enzyme Commision number 1.2.1.79: succinate-semialdehyde dehydrogenase (NADP(+)).
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 SSN A N132 Q137 R140 V262 C263 F426 N131 Q136 R139 V261 C262 F425 MOAD: Ki=0.1mM
BS02 SSN A Y3 K155 S158 Y188 Y2 K154 S157 Y187 MOAD: Ki=0.1mM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004030 aldehyde dehydrogenase [NAD(P)+] activity
GO:0004777 succinate-semialdehyde dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0036243 succinate-semialdehyde dehydrogenase (NADP+) activity

View graph for
Molecular Function
External links
PDB RCSB:4ywv, PDBe:4ywv, PDBj:4ywv
PDBsum4ywv
PubMed25888791
UniProtA0A0J9X1M8

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