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1VC9

Crystal Structure of a T.thermophilus HB8 Ap6A hydrolase E50Q mutant-Mg2+-ATP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004081molecular_functionbis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
A0005524molecular_functionATP binding
A0006167biological_processAMP biosynthetic process
A0006754biological_processATP biosynthetic process
A0016787molecular_functionhydrolase activity
A0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
A0046872molecular_functionmetal ion binding
B0004081molecular_functionbis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
B0005524molecular_functionATP binding
B0006167biological_processAMP biosynthetic process
B0006754biological_processATP biosynthetic process
B0016787molecular_functionhydrolase activity
B0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
AHIS32
AGLU46
AHOH2010
AHOH2060

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 1001
ChainResidue
ATYR66
AASN68
APRO69
AARG74
APHE110
AGLU112
AHOH2002
AHOH2005
AHOH2012
AHOH2048
AASP21
AMET23
APHE25
ALYS30
AHIS32

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP B 1002
ChainResidue
BASP21
BMET23
BPHE25
BLYS30
BHIS32
BTYR66
BASN68
BPRO69
BARG74
BPHE110
BGLU112
BHOH1003
BHOH1011
BHOH1023
BHOH1037
BHOH1045

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|Ref.2
ChainResidueDetails
AASP21
BTYR66
BARG74
BGLU112
ALYS30
AGLU46
ATYR66
AARG74
AGLU112
BASP21
BLYS30
BGLU46

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:15024014
ChainResidueDetails
AGLN50
BGLN50

220113

PDB entries from 2024-05-22

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