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4KM4

E. coli alkaline phosphatase mutant S102G/R166S in complex with inorganic phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004035molecular_functionalkaline phosphatase activity
A0004721molecular_functionphosphoprotein phosphatase activity
A0005515molecular_functionprotein binding
A0006470biological_processprotein dephosphorylation
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0030613molecular_functionoxidoreductase activity, acting on phosphorus or arsenic in donors
A0033748molecular_functionhydrogenase (acceptor) activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004035molecular_functionalkaline phosphatase activity
B0004721molecular_functionphosphoprotein phosphatase activity
B0005515molecular_functionprotein binding
B0006470biological_processprotein dephosphorylation
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0030613molecular_functionoxidoreductase activity, acting on phosphorus or arsenic in donors
B0033748molecular_functionhydrogenase (acceptor) activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AASP51
AZN502
AZN503
AZN504
AGLY102
AASP153
AASP327
ALYS328
AHIS331
AASP369
AHIS370
AHIS412

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AASP51
AASP327
AASP369
AHIS370
APO4501

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
AASP327
AHIS331
AHIS412
APO4501

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
AASP51
AASP153
ATHR155
AGLU322
APO4501

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
BASP51
BGLY102
BASP153
BASP327
BLYS328
BHIS331
BASP369
BHIS370
BHIS412
BZN502
BZN503

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BASP51
BASP327
BASP369
BHIS370
BPO4501

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BASP327
BHIS331
BHIS412
BPO4501

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 504
ChainResidue
BASP51
BASP153
BTHR155
BGLU322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphoserine intermediate
ChainResidueDetails
AGLY102
BGLY102

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AASP51
BASP51
BASP153
BTHR155
BGLU322
BASP327
BHIS331
BASP369
BHIS370
BHIS412
AASP153
ATHR155
AGLU322
AASP327
AHIS331
AASP369
AHIS370
AHIS412

Catalytic Information from CSA
site_idMCSA1
Number of Residues12
DetailsM-CSA 44
ChainResidueDetails
AASP51metal ligand
AASP369metal ligand
AHIS370metal ligand
AHIS412metal ligand
AGLY102hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
AASP153metal ligand
ATHR155metal ligand
ASER166activator, electrostatic stabiliser, hydrogen bond donor
AGLU322metal ligand
AASP327metal ligand
ALYS328metal ligand
AHIS331metal ligand

site_idMCSA2
Number of Residues12
DetailsM-CSA 44
ChainResidueDetails
BASP51metal ligand
BASP369metal ligand
BHIS370metal ligand
BHIS412metal ligand
BGLY102hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
BASP153metal ligand
BTHR155metal ligand
BSER166activator, electrostatic stabiliser, hydrogen bond donor
BGLU322metal ligand
BASP327metal ligand
BLYS328metal ligand
BHIS331metal ligand

222036

PDB entries from 2024-07-03

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