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3QBX

Crystal structure of pseudomonas aeruginosa 1,6-anhydro-n-actetylmuramic acid kinase (ANMK) bound to 1,6-anhydro-n-actetylmuramic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006040biological_processamino sugar metabolic process
A0009254biological_processpeptidoglycan turnover
A0016301molecular_functionkinase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0046677biological_processresponse to antibiotic
A0097175biological_process1,6-anhydro-N-acetyl-beta-muramic acid catabolic process
B0005524molecular_functionATP binding
B0006040biological_processamino sugar metabolic process
B0009254biological_processpeptidoglycan turnover
B0016301molecular_functionkinase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0046677biological_processresponse to antibiotic
B0097175biological_process1,6-anhydro-N-acetyl-beta-muramic acid catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AH0 A 653
ChainResidue
ATHR97
AASP182
AGLU326
AHOH394
AHIS100
AARG129
AALA140
APRO141
ALEU142
AVAL143
APHE166
AASN168

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 372
ChainResidue
AGLY10
ATHR11
ASER12
AGLY164
AGLY165
AHOH412
AHOH443

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AH0 B 654
ChainResidue
BTHR97
BHIS100
BARG129
BALA140
BPRO141
BLEU142
BVAL143
BPHE166
BASN168
BASP182
BGLU326
BHOH387
BHOH409

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 372
ChainResidue
BGLY10
BTHR11
BSER12
BGLY165
BHOH406
BHOH409
BHOH419
BHOH425

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01270
ChainResidueDetails
AGLY10
BGLY10

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PDB entries from 2024-06-12

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