Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

BioLiP

Structure of PDB 4i3x Chain G

Receptor sequence
>4i3xG (length=474) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence]
HEPMRIAGRLVDTDDRVEVRYPWNDTVVGTVPAGRAEHAREAFAIAAAYQ
PKLTRYERQKILLATAEALAARKEEISDVITLELGISKADSLYEVGRAFD
VFTLAGQMCIRDDGEIFSCDLTPHGKARKIFTMREPLTAISAITPFNHPL
NMVAHKVAPAIATNNCVVVKPTELTPMTALLLADILYEAGLPPEMLSVVT
GWPADIGMEMITNPHVDLVTFTGSVPVGKLIAANAHYKRQVLELGGNDPL
IILNDLSDDDLARAADLAVAGATKNSGQRCTAVKRILCQESVADRFVPLV
LERAKRLRFGDPMDRSTDLGTVIHEKAAALFEERVMRAAEEGADILYHPG
RSGALLPPIVVDRVPHQSDLVLEETFGPIIPIVRVPDDDDATITLSNSTA
FGLSSGVCTNDYRRMQKYIAGLKVGTVNIWEVPGYRIEMSPFGGIKDSGN
GYKEGVIEAMKSFTNVKTFSLPWP
3D structure
PDB4i3x Structure and function of phosphonoacetaldehyde dehydrogenase: the missing link in phosphonoacetate formation.
ChainG
Resolution2.07 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) N158 K181 E254 C291 E385 E465
Catalytic site (residue number reindexed from 1) N147 K170 E243 C280 E374 E454
Enzyme Commision number 1.2.1.-
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 NAD G I154 T155 P156 F157 K181 T183 P214 F232 T233 G234 S235 V238 E254 L255 C291 E385 F387 I143 T144 P145 F146 K170 T172 P203 F221 T222 G223 S224 V227 E243 L244 C280 E374 F376
BS02 PAE G R108 H159 R290 C291 R447 R97 H148 R279 C280 R436
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008911 lactaldehyde 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

View graph for
Molecular Function
External links
PDB RCSB:4i3x, PDBe:4i3x, PDBj:4i3x
PDBsum4i3x
PubMed24361046
UniProtQ92UV7|PHNY_RHIME Phosphonoacetaldehyde dehydrogenase (Gene Name=phnY)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417