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2BNF

The structure of E. coli UMP kinase in complex with UTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006225biological_processUDP biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0033862molecular_functionUMP kinase activity
A0042802molecular_functionidentical protein binding
A0044210biological_process'de novo' CTP biosynthetic process
A0046940biological_processnucleoside monophosphate phosphorylation
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006225biological_processUDP biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0033862molecular_functionUMP kinase activity
B0042802molecular_functionidentical protein binding
B0044210biological_process'de novo' CTP biosynthetic process
B0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE UTP A1242
ChainResidue
ALYS15
AASP77
AGLY80
AMSE81
ATHR138
AASN140
APRO141
APHE143
ATHR144
ATHR145
AHOH2009
ASER17
AHOH2040
AGLY18
AGLY56
AGLY57
AGLY58
APHE61
AARG62
AGLY63

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE UTP B1242
ChainResidue
BLYS15
BSER17
BGLY18
BGLU19
BGLY56
BGLY57
BGLY58
BPHE61
BARG62
BGLY63
BASP77
BGLY80
BMSE81
BTHR138
BASN140
BPRO141
BPHE143
BTHR144
BTHR145
BHOH2012
BHOH2025

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1243
ChainResidue
AGLN39
ALYS42
AGOL1244
BGLN39
BGLU46

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1244
ChainResidue
AGLN39
AGLU46
AGOL1243
BGLN39
BLYS42

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1245
ChainResidue
AGLY58
ALEU60
APHE61
AARG62

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1246
ChainResidue
AVAL192
ALEU193
ALEU197
AVAL199
AMSE200
ALEU202
AHOH2033

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1247
ChainResidue
AVAL100
AASN101
AARG127
AHOH2041

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B1243
ChainResidue
AASP210
AHIS211
BARG73

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B1244
ChainResidue
BVAL100
BASN101
BHOH2033

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2BND, ECO:0007744|PDB:2BNF, ECO:0007744|PDB:2V4Y
ChainResidueDetails
ALEU16
AGLY58
AASN59
BLEU16
BGLY58
BASN59

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0007744|PDB:2BND, ECO:0007744|PDB:2BNE, ECO:0007744|PDB:2BNF
ChainResidueDetails
AGLY63
BGLY63

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2BNE, ECO:0007744|PDB:2BNF, ECO:0007744|PDB:2V4Y
ChainResidueDetails
AHIS78
BHIS78

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15857829, ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2BND, ECO:0007744|PDB:2BNE, ECO:0007744|PDB:2BNF, ECO:0007744|PDB:2V4Y
ChainResidueDetails
AGLY139
BGLY139

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS166
ATHR172
APRO175
BLYS166
BTHR172
BPRO175

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18945668, ECO:0007744|PDB:2V4Y
ChainResidueDetails
AASP93
AALA102
BASP93
BALA102

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PDB entries from 2025-06-18

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