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4IJ5

Crystal Structure of a Novel-type Phosphoserine Phosphatase from Hydrogenobacter thermophilus TK-6

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006564biological_processL-serine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0036424molecular_functionL-phosphoserine phosphatase activity
B0005737cellular_componentcytoplasm
B0006564biological_processL-serine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0036424molecular_functionL-phosphoserine phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
AARG8
AASN15
AGLN21
AHOH402
AHOH413

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AHOH522
ALYS130
AMET184
AASN189
AHOH434

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
ATRP14
AVAL17
AARG19
BSER89
BMET91
BHOH480

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
ATRP170
AALA210
AHOH495
BARG188
BHOH433

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BMET184
BASN189
BHOH501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250
ChainResidueDetails
AHIS9
BHIS9

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS150
BHIS150

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for activity => ECO:0000250
ChainResidueDetails
AARG58
BARG58

218853

PDB entries from 2024-04-24

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