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1KYT

Crystal Structure of Thermoplasma acidophilum 0175 (APC014)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0008967molecular_functionphosphoglycolate phosphatase activity
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0008967molecular_functionphosphoglycolate phosphatase activity
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BASP8
BASP10
BASP174
BSER175
BASP178
BHOH508
BHOH510

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
ASER175
AASN177
AASP178
AHOH534
AHOH567
AASP8
AASP174

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AGLY11
AASP174
AHOH514
AHOH524
AHOH530
AHOH532
AHOH538

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
AGLU119
BGLY139
BHOH505
BHOH633
BHOH634
BHOH635

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 505
ChainResidue
AASN44
ASER138
ATYR140
AHOH537

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 506
ChainResidue
AHOH583
AHOH642

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP8
BASP8

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AASP8
BGLY11
BGLY43
BASP174
BSER175
BASP178
AASP10
AGLY11
AGLY43
AASP174
ASER175
AASP178
BASP8
BASP10

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS151
BLYS151

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PDB entries from 2024-07-24

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