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2R84

Crystal structure of PurP from Pyrococcus furiosus complexed with AMP and AICAR

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0006164biological_processpurine nucleotide biosynthetic process
A0006188biological_processIMP biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0016874molecular_functionligase activity
A0016879molecular_functionligase activity, forming carbon-nitrogen bonds
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0006164biological_processpurine nucleotide biosynthetic process
B0006188biological_processIMP biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0016874molecular_functionligase activity
B0016879molecular_functionligase activity, forming carbon-nitrogen bonds
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 600
ChainResidue
AGLU98
AGLU104
AILE284
AHOH602
AHOH621

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
AHOH894
AHIS11
AARG202
AARG287
AALA290

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 600
ChainResidue
BGLU98
BGLU104
BILE284
BHOH795
BHOH796
BHOH842

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 601
ChainResidue
BHIS11
BARG287
BALA290
BHOH837

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP A 400
ChainResidue
AILE130
ALYS132
ATYR142
AGLN173
AGLU174
ATYR175
AARG212
AHOH610
AHOH612
AHOH615
AHOH616
AHOH823
AHOH931

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMZ A 401
ChainResidue
ASER10
AHIS11
AGLY70
ASER71
AHIS75
AARG202
AASN232
AARG238
ASER240
AALA290
AHOH603
AHOH606
AHOH607
AHOH608
AHOH609
AHOH781

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP B 400
ChainResidue
BPRO116
BILE130
BLYS132
BTYR142
BGLN173
BGLU174
BTYR175
BGLU283
BHOH698
BHOH700
BHOH701
BHOH702
BHOH767

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMZ B 401
ChainResidue
BSER10
BHIS11
BGLY70
BSER71
BHIS75
BARG202
BASN232
BARG238
BSER240
BALA290
BHOH603
BHOH606
BHOH607
BHOH608
BHOH609
BHOH829

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 500
ChainResidue
ATYR142
AASP217
ATYR227
AHOH779

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 501
ChainResidue
ATYR175
ALEU177
AILE213
APHE221
AHOH834
AHOH835

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD B 501
ChainResidue
BTYR175
BLEU177
BILE213
BPHE221
BMET223
BHOH856

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01163","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-12-24

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