Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5CDO

3.15A structure of QPT-1 with S.aureus DNA gyrase and DNA

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
C0003677molecular_functionDNA binding
C0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
C0005524molecular_functionATP binding
C0006259biological_processDNA metabolic process
C0006265biological_processDNA topological change
D0003677molecular_functionDNA binding
D0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
D0005524molecular_functionATP binding
D0006265biological_processDNA topological change
R0003677molecular_functionDNA binding
R0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
R0005524molecular_functionATP binding
R0006259biological_processDNA metabolic process
R0006265biological_processDNA topological change
S0003677molecular_functionDNA binding
S0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
S0005524molecular_functionATP binding
S0006265biological_processDNA topological change
T0003677molecular_functionDNA binding
T0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
T0005524molecular_functionATP binding
T0006259biological_processDNA metabolic process
T0006265biological_processDNA topological change
U0003677molecular_functionDNA binding
U0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
U0005524molecular_functionATP binding
U0006265biological_processDNA topological change
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 501
ChainResidue
AARG429
CARG429

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 502
ChainResidue
ATYR322
ALYS323
ATHR325
AGLN328

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 503
ChainResidue
APRO157
AARG47
AARG48
AGLU156

site_idAC4
Number of Residues6
Detailsbinding site for residue MN B 701
ChainResidue
BASP508
BASP510
BHOH801
BHOH802
BHOH805
EHOH2202

site_idAC5
Number of Residues3
Detailsbinding site for residue NA C 501
ChainResidue
CGLY152
CASN153
CGLU154

site_idAC6
Number of Residues4
Detailsbinding site for residue NA C 502
ChainResidue
CTYR322
CLYS323
CTHR325
CGLN328

site_idAC7
Number of Residues6
Detailsbinding site for residue MN D 1001
ChainResidue
DASP508
DASP510
DHOH1101
DHOH1102
DHOH1103
DHOH1104

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL D 1002
ChainResidue
DASN474
DASN475
DASN476
EDG2013

site_idAC9
Number of Residues3
Detailsbinding site for residue GOL D 1003
ChainResidue
ASER297
DSER445
DGLY446

site_idAD1
Number of Residues8
Detailsbinding site for residue 53M E 2101
ChainResidue
BGLY436
BASP437
BARG458
CPTR123
EDC8
EDG2009
FDC2012
FDG2013

site_idAD2
Number of Residues10
Detailsbinding site for residue 53L F 2101
ChainResidue
APTR123
DGLY436
DASP437
DARG458
DGLY459
EDC2012
EDG2013
FDC8
FDG2009
FHOH2202

site_idAD3
Number of Residues3
Detailsbinding site for residue NA R 501
ChainResidue
RTYR322
RTHR325
RGLN328

site_idAD4
Number of Residues6
Detailsbinding site for residue MN S 6001
ChainResidue
SASP508
SASP510
SHOH6103
SHOH6104
SHOH6106
SHOH6107

site_idAD5
Number of Residues10
Detailsbinding site for residue 50M S 6002
ChainResidue
SGLY436
SASP437
SARG458
SGLY459
SHOH6102
TPTR123
VDC2012
VDG2013
WDC8
WDG2009

site_idAD6
Number of Residues3
Detailsbinding site for residue SO4 T 501
ChainResidue
RARG429
TARG429
TARG432

site_idAD7
Number of Residues5
Detailsbinding site for residue SO4 T 502
ChainResidue
TPRO44
TARG47
TGLU156
TPRO157
TSER158

site_idAD8
Number of Residues4
Detailsbinding site for residue NA T 503
ChainResidue
TTYR322
TTHR325
TGLN328
THOH615

site_idAD9
Number of Residues6
Detailsbinding site for residue MN U 5001
ChainResidue
UASP508
UASP510
UHOH5101
UHOH5102
UHOH5107
VHOH2102

site_idAE1
Number of Residues2
Detailsbinding site for residue GOL U 5002
ChainResidue
UASN476
WDG2013

site_idAE2
Number of Residues3
Detailsbinding site for residue GOL U 5003
ChainResidue
UGLY446
UARG447
UTRP592

site_idAE3
Number of Residues8
Detailsbinding site for residue 53M W 2101
ChainResidue
UGLY459
VDC8
VDG2009
WDC2012
WDG2013
UGLY436
UASP437
UARG458

Functional Information from PROSITE/UniProt
site_idPS00177
Number of Residues9
DetailsTOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG
ChainResidueDetails
BLEU433-GLY441

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01898
ChainResidueDetails
BGLU435
UGLU435
UASP508
UASP510
BASP508
BASP510
DGLU435
DASP508
DASP510
SGLU435
SASP508
SASP510

site_idSWS_FT_FI2
Number of Residues8
DetailsSITE: Interaction with DNA => ECO:0000255|HAMAP-Rule:MF_01898
ChainResidueDetails
BLYS460
BASN463
DLYS460
DASN463
SLYS460
SASN463
ULYS460
UASN463

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon