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1PKK

Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006226biological_processdUMP biosynthetic process
A0006229biological_processdUTP biosynthetic process
A0008829molecular_functiondCTP deaminase activity
A0009117biological_processnucleotide metabolic process
A0016787molecular_functionhydrolase activity
A0033973molecular_functiondCTP deaminase (dUMP-forming) activity
B0000166molecular_functionnucleotide binding
B0006226biological_processdUMP biosynthetic process
B0006229biological_processdUTP biosynthetic process
B0008829molecular_functiondCTP deaminase activity
B0009117biological_processnucleotide metabolic process
B0016787molecular_functionhydrolase activity
B0033973molecular_functiondCTP deaminase (dUMP-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DCP B 293
ChainResidue
BARG117
BHOH557
BSER118
BSER119
BARG122
BHIS128
BPHE138
BTHR143
BGLU145
BHOH455

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 294
ChainResidue
AASP25
AVAL27
AGLY28
AASP33
AARG160
BASN87
BHOH571

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 295
ChainResidue
BGLU39
BLEU97
BGLY98
BTHR99
BHOH344
BHOH442

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 296
ChainResidue
AASP174
ATYR177
ASER178
AHOH508
BLYS60
BILE61
BLYS62

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 297
ChainResidue
BARG16
BGLU105
BLEU106
BHOH376
BHOH524

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 298
ChainResidue
AASN23
AHOH471

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 299
ChainResidue
BASP38
BASN101
BASN158

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 300
ChainResidue
BTHR35
BHOH515

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P28248, ECO:0000255|HAMAP-Rule:MF_00146
ChainResidueDetails
AGLU145
BGLU145

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146
ChainResidueDetails
AARG117
AGLN163
BARG117
BGLN163

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:12909016
ChainResidueDetails
AHIS128
BHIS128

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|Ref.6
ChainResidueDetails
AGLY132
BGLY132

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|Ref.6
ChainResidueDetails
AASP135
ATYR177
ALYS184
AGLN188
BASP135
BTYR177
BLYS184
BGLN188

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:12909016, ECO:0000305|Ref.6
ChainResidueDetails
ATHR143
BTHR143

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Important for bifunctional activity => ECO:0000255|HAMAP-Rule:MF_00146
ChainResidueDetails
AGLY132
BGLY132

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
AASP135
AGLY137

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dup
ChainResidueDetails
BASP135
BGLY137

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PDB entries from 2024-10-16

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