5ZOD

Crystal Structure of hFen1 in apo form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003824	molecular_function	catalytic activity
A	0004518	molecular_function	nuclease activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 401

Chain	Residue
A	HOH504
A	HOH512
A	HOH513
A	HOH542
A	HOH547
A	HOH633

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 402

Chain	Residue
A	ASP233
A	TYR234
A	HOH542
A	GLU160
A	ASP179
A	ASP181

---

site_id	AC3
Number of Residues	5
Details	binding site for residue K A 403

Chain	Residue
A	ALA17
A	ARG19
A	GLU206
A	HIS208
A	HOH544

---

site_id	AC4
Number of Residues	4
Details	binding site for residue K A 404

Chain	Residue
A	ASN219
A	GLN220
A	GLU221
A	HOH649

---

site_id	AC5
Number of Residues	5
Details	binding site for residue K A 405

Chain	Residue
A	ASP225
A	HIS276
A	HIS280
A	HOH506
A	HOH603

---

site_id	AC6
Number of Residues	5
Details	binding site for residue K A 406

Chain	Residue
A	LEU289
A	ASP290
A	PRO291
A	HOH594
A	HOH638

---

Functional Information from PROSITE/UniProt

site_id	PS00841
Number of Residues	15
Details	XPG_1 XPG protein signature 1. IKPvYVFDGkpPqLK

Chain	Residue	Details
A	ILE79-LYS93

---

site_id	PS00842
Number of Residues	15
Details	XPG_2 XPG protein signature 2. GIPYLdAPsEAEASC

Chain	Residue	Details
A	GLY149-CYS163

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1

Chain	Residue	Details
A	ASP34

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING:

Chain	Residue	Details
A	GLY231
A	ARG47
A	ARG70

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7

Chain	Residue	Details
A	GLU158
A	ASP86

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD

Chain	Residue	Details
A	ASP181
A	GLU160

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD

Chain	Residue	Details
A	ASP179

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:5ZOD

Chain	Residue	Details
A	ASP233

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856

Chain	Residue	Details
A	ARG192
A	ARG19
A	ARG100
A	ARG104

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS80

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CDK2 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856

Chain	Residue	Details
A	SER187

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER197

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER293
A	SER255

---