3Q8M

Crystal Structure of Human Flap Endonuclease FEN1 (D181A) in complex with substrate 5'-flap DNA 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
B	0003677	molecular_function	DNA binding
B	0003824	molecular_function	catalytic activity
B	0004518	molecular_function	nuclease activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K B 1101

Chain	Residue
B	SER237
B	ILE238
D	DT5

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 1102

Chain	Residue
A	SER237
A	ILE241
G	DT5

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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

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

Chain	Residue	Details
A	GLY149-CYS163

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1

Chain	Residue	Details
A	ASP34
B	ASP34

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	ARG47
A	ARG70
A	GLY231
B	ARG47
B	ARG70
B	GLY231

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7

Chain	Residue	Details
A	ASP86
A	GLU158
B	ASP86
B	GLU158

---

site_id	SWS_FT_FI4
Number of Residues	4
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	ALA181
B	GLU160
B	ALA181

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD

Chain	Residue	Details
A	ASP179
B	ASP179

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:5ZOD

Chain	Residue	Details
A	ASP233
B	ASP233

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site_id	SWS_FT_FI7
Number of Residues	8
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
B	ARG19
B	ARG100
B	ARG104
B	ARG192

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS80
B	LYS80

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site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine; by CDK2 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856

Chain	Residue	Details
A	SER187
B	SER187

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site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER197
B	SER197

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site_id	SWS_FT_FI11
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER255
A	SER293
A	SER335
B	SER255
B	SER293
B	SER335

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR336
B	THR336

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