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2YYE

Crystal structure of selenophosphate synthetase from Aquifex aeolicus complexed with AMPCPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004756molecular_functionselenide, water dikinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016260biological_processselenocysteine biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004756molecular_functionselenide, water dikinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0016260biological_processselenocysteine biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO B 701
ChainResidue
AASP60
AHOH931
BHIS132

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 702
ChainResidue
AASP44
AASP83
AASP219
AHOH859
AHOH918

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 703
ChainResidue
AASP83
AHOH859
AHOH932
AASP60

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 704
ChainResidue
AASP44
ATHR58
AASP60
AASP83
AHOH804
AHOH860
AHOH931

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 705
ChainResidue
AASP43
AASP44
AALA86
AMET87
AILE155
ACYS217

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO A 801
ChainResidue
AHIS132
BASP60
BHOH991

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 802
ChainResidue
BASP44
BASP83
BASP219
BHOH902
BHOH1049

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO B 803
ChainResidue
BASP60
BASP83
BHOH1027
BHOH1049

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO B 804
ChainResidue
BASP44
BTHR58
BASP60
BASP83
BHOH903
BHOH917
BHOH991

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 805
ChainResidue
BASP43
BASP44
BALA86
BMET87
BILE155
BCYS217

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 901
ChainResidue
ALYS259
BLYS179
BGLU183
BLYS260
BILE261
BTYR262

site_idBC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE APC A 501
ChainResidue
ALYS16
ALEU22
ALEU26
AGLY42
AASP43
AASP44
AASP60
AASP83
ATHR221
AGLY222
APHE223
AHOH833
AHOH859
AHOH860
AHOH918
AHOH928
AHOH931
AHOH932
BALA96
BSER98
BGLY130
BGLY131
BHIS132
BTHR133
BHOH921
BHOH1048

site_idBC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE APC B 601
ChainResidue
BHOH902
BHOH917
BHOH935
BHOH942
BHOH944
BHOH949
BHOH982
BHOH991
BHOH1049
AALA96
ASER98
AGLY130
AGLY131
AHIS132
ATHR133
AHOH822
AHOH929
BLEU22
BLEU26
BGLY42
BASP43
BASP44
BASP60
BASP83
BTHR221
BGLY222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00625","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00625","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00625","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_00625","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsNon-standard residue: {"description":"Selenocysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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