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1J97

Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0006564biological_processL-serine biosynthetic process
A0016787molecular_functionhydrolase activity
A0036424molecular_functionL-phosphoserine phosphatase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0006564biological_processL-serine biosynthetic process
B0016787molecular_functionhydrolase activity
B0036424molecular_functionL-phosphoserine phosphatase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 220
ChainResidue
ABFD11
AASP13
AASP167
AHOH808
AHOH828

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 720
ChainResidue
BHOH821
BBFD511
BASP513
BASP667
BHOH809

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 230
ChainResidue
BASN607
BLYS610
BGLU611
BLYS691
BCYS697
BGLU699
BHOH901
BHOH1057

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 240
ChainResidue
ALYS4
BASN548
BGLU550
BHOH804
BHOH832
BHOH928

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:11342136, ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918
ChainResidueDetails
ABFD11
BBFD511

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11342136, ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918
ChainResidueDetails
AASP13
BASP513

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:11342136, ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918
ChainResidueDetails
ABFD11
BGLU520
BARG556
BSER599
BLYS644
BASP667
AASP13
AGLU20
AARG56
ASER99
ALYS144
AASP167
BBFD511
BASP513

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051918
ChainResidueDetails
AASN170
BASN670

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 727
ChainResidueDetails
ABFD11covalently attached, metal ligand, nucleofuge, nucleophile
APHE12electrostatic stabiliser
AASP13metal ligand, proton acceptor, proton donor
AGLY100electrostatic stabiliser
ALYS144electrostatic stabiliser
AASP171electrostatic stabiliser, metal ligand

site_idMCSA2
Number of Residues6
DetailsM-CSA 727
ChainResidueDetails
BBFD511covalently attached, metal ligand, nucleofuge, nucleophile
BPHE512electrostatic stabiliser
BASP513metal ligand, proton acceptor, proton donor
BGLY600electrostatic stabiliser
BLYS644electrostatic stabiliser
BASP671electrostatic stabiliser, metal ligand

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PDB entries from 2024-08-07

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