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1KYT

Crystal Structure of Thermoplasma acidophilum 0175 (APC014)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005829cellular_componentcytosol
A0008967molecular_functionphosphoglycolate phosphatase activity
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005829cellular_componentcytosol
B0008967molecular_functionphosphoglycolate phosphatase activity
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase 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
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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