3Q8K

Crystal Structure of Human Flap Endonuclease FEN1 (WT) in complex with product 5'-flap DNA, SM3+, and K+

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 SM A 1001

Chain	Residue
A	ASP86
A	GLU160
A	HOH598
A	HOH693
A	HOH742
E	DT2

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SM A 1002

Chain	Residue
A	OH347
A	HOH555
E	DT2
A	GLU160
A	ASP179
A	ASP181

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SM A 1003

Chain	Residue
A	GLU57
A	GLU285
A	GLU313
A	GLN342
A	HOH767
A	HOH768
A	HOH769

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SM A 1004

Chain	Residue
A	GLU57
A	GLU59
A	GLU313
A	GLN342
A	HOH764
A	HOH765
A	HOH766

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 1101

Chain	Residue
A	SER237
A	ILE238
A	ILE241
A	HOH627
D	DT5
D	HOH628

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OH A 347

Chain	Residue
A	GLY2
A	ASP179
A	ASP181
A	ASP233
A	HOH555
A	SM1002
E	DT2
E	HOH455

---

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	ARG47
A	ARG70
A	GLY231

---

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	ASP86
A	GLU158

---

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	GLU160
A	ASP181

---

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	ARG19
A	ARG100
A	ARG104
A	ARG192

---

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	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER255
A	SER293
A	SER335

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR336

---