5LB5

Crystal structure of human RECQL5 helicase in complex with ADP/Mg (tricilinc form).

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0004386	molecular_function	helicase activity
A	0005524	molecular_function	ATP binding
A	0006310	biological_process	DNA recombination
B	0003676	molecular_function	nucleic acid binding
B	0004386	molecular_function	helicase activity
B	0005524	molecular_function	ATP binding
B	0006310	biological_process	DNA recombination
C	0003676	molecular_function	nucleic acid binding
C	0004386	molecular_function	helicase activity
C	0005524	molecular_function	ATP binding
C	0006310	biological_process	DNA recombination
D	0003676	molecular_function	nucleic acid binding
D	0004386	molecular_function	helicase activity
D	0005524	molecular_function	ATP binding
D	0006310	biological_process	DNA recombination

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 501

Chain	Residue
A	CYS411
A	CYS427
A	CYS431
A	CYS434

---

site_id	AC2
Number of Residues	4
Details	binding site for residue DMS A 502

Chain	Residue
A	ALA193
A	ALA195
A	TYR344
A	PHE420

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 503

Chain	Residue
A	HOH637
A	HOH672
A	HOH675
A	HOH691
A	ADP504

---

site_id	AC4
Number of Residues	18
Details	binding site for residue ADP A 504

Chain	Residue
A	PHE26
A	SER28
A	PHE29
A	LYS30
A	GLN34
A	PRO53
A	THR54
A	GLY55
A	ALA56
A	GLY57
A	LYS58
A	SER59
A	MG503
A	HOH610
A	HOH629
A	HOH637
A	HOH663
A	HOH675

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN B 501

Chain	Residue
B	CYS411
B	CYS427
B	CYS431
B	CYS434

---

site_id	AC6
Number of Residues	3
Details	binding site for residue DMS B 502

Chain	Residue
B	TYR265
B	ILE317
B	SER318

---

site_id	AC7
Number of Residues	5
Details	binding site for residue MG B 503

Chain	Residue
B	ADP504
B	HOH605
B	HOH630
B	HOH684
B	HOH686

---

site_id	AC8
Number of Residues	18
Details	binding site for residue ADP B 504

Chain	Residue
B	PHE26
B	SER28
B	PHE29
B	LYS30
B	GLN34
B	PRO53
B	THR54
B	GLY55
B	ALA56
B	GLY57
B	LYS58
B	SER59
B	MG503
B	HOH610
B	HOH613
B	HOH630
B	HOH674
B	HOH684

---

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN C 501

Chain	Residue
C	CYS411
C	CYS427
C	CYS431
C	CYS434

---

site_id	AD1
Number of Residues	4
Details	binding site for residue MG C 502

Chain	Residue
C	ADP503
C	HOH615
C	HOH657
C	HOH668

---

site_id	AD2
Number of Residues	15
Details	binding site for residue ADP C 503

Chain	Residue
C	PHE26
C	SER28
C	LYS30
C	GLN34
C	PRO53
C	THR54
C	GLY55
C	ALA56
C	GLY57
C	LYS58
C	SER59
C	MG502
C	HOH615
C	HOH653
C	HOH657

---

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN D 501

Chain	Residue
D	CYS411
D	CYS427
D	CYS431
D	CYS434

---

site_id	AD4
Number of Residues	3
Details	binding site for residue DMS D 502

Chain	Residue
D	TYR265
D	SER318
D	PHE319

---

site_id	AD5
Number of Residues	5
Details	binding site for residue MG D 503

Chain	Residue
D	ADP504
D	HOH610
D	HOH618
D	HOH649
D	HOH660

---

site_id	AD6
Number of Residues	13
Details	binding site for residue ADP D 504

Chain	Residue
D	GLN34
D	PRO53
D	GLY55
D	ALA56
D	GLY57
D	LYS58
D	SER59
D	MG503
D	HOH610
D	HOH618
D	PHE26
D	SER28
D	LYS30

---

Functional Information from PROSITE/UniProt

site_id	PS00690
Number of Residues	10
Details	DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. SyLVVDEAHC

Chain	Residue	Details
A	SER152-CYS161

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000305|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA

Chain	Residue	Details
A	PHE26
B	PHE26
B	SER28
B	LYS30
B	GLN34
B	GLY55
B	ALA56
B	GLY57
B	LYS58
B	SER59
C	PHE26
A	SER28
C	SER28
C	LYS30
C	GLN34
C	GLY55
C	ALA56
C	GLY57
C	LYS58
C	SER59
D	PHE26
D	SER28
A	LYS30
D	LYS30
D	GLN34
D	GLY55
D	ALA56
D	GLY57
D	LYS58
D	SER59
A	GLN34
A	GLY55
A	ALA56
A	GLY57
A	LYS58
A	SER59

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744|PDB:5LB5

Chain	Residue	Details
A	PRO53
B	PRO53
C	PRO53
D	PRO53

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LB8, ECO:0007744|PDB:5LBA

Chain	Residue	Details
A	CYS411
D	CYS411
D	CYS431
D	CYS434
A	CYS431
A	CYS434
B	CYS411
B	CYS431
B	CYS434
C	CYS411
C	CYS431
C	CYS434

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA

Chain	Residue	Details
A	CYS427
B	CYS427
C	CYS427
D	CYS427

---