1HQC

STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000400	molecular_function	four-way junction DNA binding
A	0003677	molecular_function	DNA binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006281	biological_process	DNA repair
A	0006310	biological_process	DNA recombination
A	0006974	biological_process	DNA damage response
A	0009378	molecular_function	four-way junction helicase activity
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0048476	cellular_component	Holliday junction resolvase complex
B	0000166	molecular_function	nucleotide binding
B	0000400	molecular_function	four-way junction DNA binding
B	0003677	molecular_function	DNA binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006281	biological_process	DNA repair
B	0006310	biological_process	DNA recombination
B	0006974	biological_process	DNA damage response
B	0009378	molecular_function	four-way junction helicase activity
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0048476	cellular_component	Holliday junction resolvase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	THR52

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG B 402

Chain	Residue
B	VAL68

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ADE A 501

Chain	Residue
A	TYR14
A	ILE15
A	THR53
A	ARG179
A	LYS208

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ADE B 502

Chain	Residue
B	ILE15
B	TYR168
B	LYS208
B	ARG7
B	TYR14

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11171970, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS

Chain	Residue	Details
A	TYR14
B	TYR14

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11171970, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS

Chain	Residue	Details
A	ILE15
B	ILE15

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1IXR

Chain	Residue	Details
A	GLY48
B	GLY48

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1IXR, ECO:0000312|PDB:1IXS

Chain	Residue	Details
A	LYS51
A	THR53
B	LYS51
B	THR53

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016

Chain	Residue	Details
A	THR52
A	ARG297
A	ARG302
B	THR52
B	ARG297
B	ARG302

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:12408833

Chain	Residue	Details
A	ASP97
A	THR146
B	ASP97
B	THR146

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:11171970, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS

Chain	Residue	Details
A	TYR168
B	TYR168

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site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000305|PubMed:12408833

Chain	Residue	Details
A	ARG205
B	ARG205

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10464259, 11171970

Chain	Residue	Details
A	THR146
A	ARG205

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site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10464259, 11171970

Chain	Residue	Details
B	THR146
B	ARG205

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
A	LYS51
A	THR52
A	ASP97
A	THR146	electrostatic stabiliser
A	ARG205	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 780

Chain	Residue	Details
B	LYS51
B	THR52
B	ASP97
B	THR146	electrostatic stabiliser
B	ARG205	electrostatic stabiliser

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