Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DDV

Thermotoga maritima reverse gyrase, triclinic form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0003689	molecular_function	DNA clamp loader activity
A	0003916	molecular_function	DNA topoisomerase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006265	biological_process	DNA topological change
A	0006268	biological_process	DNA unwinding involved in DNA replication
A	0006338	biological_process	chromatin remodeling
A	0008094	molecular_function	ATP-dependent activity, acting on DNA
A	0008270	molecular_function	zinc ion binding
A	0009378	molecular_function	four-way junction helicase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0034335	molecular_function	DNA negative supercoiling activity
A	0036121	molecular_function	double-stranded DNA helicase activity
A	0046872	molecular_function	metal ion binding
A	0061749	molecular_function	forked DNA-dependent helicase activity
A	0061775	molecular_function	cohesin loader activity
A	0140584	molecular_function	chromatin extrusion motor activity
A	0140588	biological_process	chromatin looping
A	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
A	0140849	molecular_function	ATP-dependent H2AZ histone chaperone activity
A	0160097	molecular_function	reverse gyrase activity
A	1990518	molecular_function	single-stranded 3'-5' DNA helicase activity
B	0003676	molecular_function	nucleic acid binding
B	0003677	molecular_function	DNA binding
B	0003689	molecular_function	DNA clamp loader activity
B	0003916	molecular_function	DNA topoisomerase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006265	biological_process	DNA topological change
B	0006268	biological_process	DNA unwinding involved in DNA replication
B	0006338	biological_process	chromatin remodeling
B	0008094	molecular_function	ATP-dependent activity, acting on DNA
B	0008270	molecular_function	zinc ion binding
B	0009378	molecular_function	four-way junction helicase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0034335	molecular_function	DNA negative supercoiling activity
B	0036121	molecular_function	double-stranded DNA helicase activity
B	0046872	molecular_function	metal ion binding
B	0061749	molecular_function	forked DNA-dependent helicase activity
B	0061775	molecular_function	cohesin loader activity
B	0140584	molecular_function	chromatin extrusion motor activity
B	0140588	biological_process	chromatin looping
B	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
B	0140849	molecular_function	ATP-dependent H2AZ histone chaperone activity
B	0160097	molecular_function	reverse gyrase activity
B	1990518	molecular_function	single-stranded 3'-5' DNA helicase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 2001

Chain	Residue
A	CYS621
A	CYS624
A	CYS635
A	CYS638

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 2002

Chain	Residue
A	CYS11
A	CYS14
A	CYS29
A	CYS32

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 2001

Chain	Residue
B	CYS624
B	CYS635
B	CYS638
B	CYS621

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 2002

Chain	Residue
B	CYS11
B	CYS14
B	CYS29
B	CYS32

Functional Information from PROSITE/UniProt

site_id	PS00572
Number of Residues	9
Details	GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LLVLENGVN

Chain	Residue	Details
A	LEU778-ASN786

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	76
Details	ZN_FING: RG N-terminal-type => ECO:0000255\|PROSITE-ProRule:PRU01380, ECO:0000269\|PubMed:23209025

Chain	Residue	Details
A	MET1-SER39
B	MET1-SER39

site_id	SWS_FT_FI2
Number of Residues	54
Details	ZN_FING: RG C-terminal-type => ECO:0000255\|PROSITE-ProRule:PRU01381, ECO:0000269\|PubMed:23209025

Chain	Residue	Details
A	LEU618-ASP645
B	LEU618-ASP645

site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255\|PROSITE-ProRule:PRU01383, ECO:0000305\|PubMed:18614530

Chain	Residue	Details
A	TYR851
B	TYR851

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: 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

Chain	Residue	Details
A	CYS11
B	CYS14
B	CYS29
B	CYS32
B	CYS621
B	CYS624
B	CYS635
B	CYS638
A	CYS14
A	CYS29
A	CYS32
A	CYS621
A	CYS624
A	CYS635
A	CYS638
B	CYS11

site_id	SWS_FT_FI5
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269\|PubMed:21627332, ECO:0007744\|PDB:3P4X

Chain	Residue	Details
A	PHE75
B	GLY103
B	GLY105
B	LYS106
B	THR107
B	THR108
A	ASP78
A	GLY103
A	GLY105
A	LYS106
A	THR107
A	THR108
B	PHE75
B	ASP78

site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01125

Chain	Residue	Details
A	GLN83
A	ALA100
A	GLU548
A	ASP668
B	GLN83
B	ALA100
B	GLU548
B	ASP668

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)