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3NUH

A domain insertion in E. coli GyrB adopts a novel fold that plays a critical role in gyrase function

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005524molecular_functionATP binding
A0006259biological_processDNA metabolic process
A0006265biological_processDNA topological change
B0003677molecular_functionDNA binding
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005524molecular_functionATP binding
B0006265biological_processDNA topological change
Functional Information from PROSITE/UniProt
site_idPS00177
Number of Residues9
DetailsTOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG
ChainResidueDetails
BLEU422-GLY430

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000305|PubMed:12051843, ECO:0000305|PubMed:18642932
ChainResidueDetails
BGLU424
BASP498
BASP500

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Interaction with DNA => ECO:0000255|HAMAP-Rule:MF_01898
ChainResidueDetails
BLYS449
BASN452

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 745
ChainResidueDetails
AARG32electrostatic stabiliser
AHIS78proton acceptor
ATYR122metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor

222415

PDB entries from 2024-07-10

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