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1YV9

Crystal structure of a HAD-like phosphatase from Enterococcus faecalis V583

Functional Information from GO Data
ChainGOidnamespacecontents
A0004035molecular_functionalkaline phosphatase activity
A0008967molecular_functionphosphoglycolate phosphatase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004035molecular_functionalkaline phosphatase activity
B0008967molecular_functionphosphoglycolate phosphatase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 3001
ChainResidue
AASP11
ATHR44
AASN45
ALYS183
AHOH3044

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 3002
ChainResidue
AHIS195
AHOH3003
AHOH3060
ATYR72
ALEU76
AASP80
AARG191

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 3003
ChainResidue
BASP11
BTHR44
BASN45
BLYS183
BHOH3053
BHOH3079

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 3004
ChainResidue
BTYR72
BASP80
BARG191
BHIS195
BHOH3005
BHOH3025

Functional Information from PROSITE/UniProt
site_idPS00761
Number of Residues14
DetailsSPASE_I_3 Signal peptidases I signature 3. VIMVGDNYetDiqS
ChainResidueDetails
AVAL203-SER216

219869

PDB entries from 2024-05-15

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