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2ZAU

Crystal structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004756molecular_functionselenide, water dikinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016260biological_processselenocysteine biosynthetic process
A0016301molecular_functionkinase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004756molecular_functionselenide, water dikinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0016260biological_processselenocysteine biosynthetic process
B0016301molecular_functionkinase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004756molecular_functionselenide, water dikinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0016260biological_processselenocysteine biosynthetic process
C0016301molecular_functionkinase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 C 901
ChainResidue
ALYS179
CLYS179
CLYS182
CPRO263
CLYS264

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 902
ChainResidue
AHOH1222
CLYS179
ALYS179
ALYS182
APRO263
ALYS264

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 903
ChainResidue
BLYS179
BLYS182
BLYS264
BHOH1244

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00625
ChainResidueDetails
AILE41
AASP60
BILE41
BASP60
CILE41
CASP60

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00625
ChainResidueDetails
AASP44
CASP83
CGLY131
CASP219
AASP83
AGLY131
AASP219
BASP44
BASP83
BGLY131
BASP219
CASP44

223166

PDB entries from 2024-07-31

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