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3KC2

Crystal structure of mitochondrial HAD-like phosphatase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003674molecular_functionmolecular_function
A0005739cellular_componentmitochondrion
A0008150biological_processbiological_process
A0016787molecular_functionhydrolase activity
A0046474biological_processglycerophospholipid biosynthetic process
B0003674molecular_functionmolecular_function
B0005739cellular_componentmitochondrion
B0008150biological_processbiological_process
B0016787molecular_functionhydrolase activity
B0046474biological_processglycerophospholipid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 A 353
ChainResidue
AASP19
AHOH894
AHOH895
AILE20
AASP21
ATHR52
AASN53
AGLY54
ALYS246
AMG355
AHOH893

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 354
ChainResidue
ALEU225
AARG228
AHOH479
AHOH544
AHOH684
AHOH862
BARG229

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 355
ChainResidue
AASP19
AASP21
AASP298
APO4353
AHOH893
AHOH894

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 353
ChainResidue
BASP19
BASP21
BASP298
BPO4354
BHOH891
BHOH892

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 B 354
ChainResidue
BASP19
BILE20
BASP21
BTHR52
BASN53
BGLY54
BLYS246
BMG353
BHOH454
BHOH548
BHOH891
BHOH892

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 355
ChainResidue
AARG229
BLEU225
BARG228
BHOH447
BHOH602
BHOH686
BHOH787

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 356
ChainResidue
AGLY134
AGLN139
BGLY134
BGLN139
BHOH362
BHOH429

221051

PDB entries from 2024-06-12

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