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4DDX

Thermotoga maritima reverse gyrase, primitive monoclinic form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003916molecular_functionDNA topoisomerase activity
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006265biological_processDNA topological change
A0006268biological_processDNA unwinding involved in DNA replication
A0008094molecular_functionATP-dependent activity, acting on DNA
A0008270molecular_functionzinc ion binding
A0016887molecular_functionATP hydrolysis activity
A0046872molecular_functionmetal ion binding
A0160097molecular_functionreverse gyrase activity
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003916molecular_functionDNA topoisomerase activity
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006265biological_processDNA topological change
B0006268biological_processDNA unwinding involved in DNA replication
B0008094molecular_functionATP-dependent activity, acting on DNA
B0008270molecular_functionzinc ion binding
B0016887molecular_functionATP hydrolysis activity
B0046872molecular_functionmetal ion binding
B0160097molecular_functionreverse gyrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1201
ChainResidue
ACYS621
ACYS624
ACYS635
ACYS638

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1202
ChainResidue
ACYS11
ACYS14
ACYS29
ACYS32

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1201
ChainResidue
BCYS624
BCYS635
BCYS638
BCYS621

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1202
ChainResidue
BCYS11
BCYS14
BCYS29
BCYS32

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LLVLENGVN
ChainResidueDetails
ALEU778-ASN786

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues76
DetailsZN_FING: RG N-terminal-type => ECO:0000255|PROSITE-ProRule:PRU01380, ECO:0000269|PubMed:23209025
ChainResidueDetails
AMET1-SER39
BMET1-SER39

site_idSWS_FT_FI2
Number of Residues54
DetailsZN_FING: RG C-terminal-type => ECO:0000255|PROSITE-ProRule:PRU01381, ECO:0000269|PubMed:23209025
ChainResidueDetails
ALEU618-ASP645
BLEU618-ASP645

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000305|PubMed:18614530
ChainResidueDetails
ATYR851
BTYR851

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01125, ECO:0000269|PubMed:23209025, ECO:0000312|PDB:7FSE, ECO:0000312|PDB:7FSF, ECO:0000312|PDB:8OFB, ECO:0007744|PDB:4DDT, ECO:0007744|PDB:4DDU, ECO:0007744|PDB:4DDV, ECO:0007744|PDB:4DDW, ECO:0007744|PDB:4DDX
ChainResidueDetails
ACYS11
BCYS14
BCYS29
BCYS32
BCYS621
BCYS624
BCYS635
BCYS638
ACYS14
ACYS29
ACYS32
ACYS621
ACYS624
ACYS635
ACYS638
BCYS11

site_idSWS_FT_FI5
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:21627332, ECO:0007744|PDB:3P4X
ChainResidueDetails
APHE75
BGLY103
BGLY105
BLYS106
BTHR107
BTHR108
AASP78
AGLY103
AGLY105
ALYS106
ATHR107
ATHR108
BPHE75
BASP78

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01125
ChainResidueDetails
AGLN83
AALA100
AGLU548
AASP668
BGLN83
BALA100
BGLU548
BASP668

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PDB entries from 2024-07-24

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