6W2P

APE1 endonuclease product complex L104R

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	0004519	molecular_function	endonuclease activity
A	0006281	biological_process	DNA repair
B	0003677	molecular_function	DNA binding
B	0003824	molecular_function	catalytic activity
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0006281	biological_process	DNA repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 401

Chain	Residue
A	GLU96
A	HOH509
A	HOH578
D	3DR1
P	DC10

---

site_id	AC2
Number of Residues	7
Details	binding site for residue EDO A 402

Chain	Residue
A	HOH527
A	HOH611
A	HOH648
A	LEU44
A	TYR45
A	ASN277
A	HOH505

---

site_id	AC3
Number of Residues	5
Details	binding site for residue EDO B 401

Chain	Residue
B	ASP189
B	PHE192
B	GLY239
B	PHE240
B	HOH552

---

Functional Information from PROSITE/UniProt

site_id	PS00726
Number of Residues	10
Details	AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK

Chain	Residue	Details
A	PRO89-LYS98

---

site_id	PS00727
Number of Residues	17
Details	AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW

Chain	Residue	Details
A	ASP251-TRP267

---

site_id	PS00728
Number of Residues	12
Details	AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS

Chain	Residue	Details
A	ASN277-SER288

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15380100

Chain	Residue	Details
B	TYR171
A	TYR171

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9351835, ECO:0007744|PDB:1BIX

Chain	Residue	Details
B	ASP210
A	ASP210

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764

Chain	Residue	Details
A	HIS309
B	HIS309

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00764

Chain	Residue	Details
A	ASP210
A	ASN212
A	ASP308
A	HIS309
B	ASN68
B	GLU96
B	ASP210
B	ASN212
B	ASP308
B	HIS309
A	ASN68
A	GLU96

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:8932375

Chain	Residue	Details
B	ASN212
A	ASN212

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799

Chain	Residue	Details
B	ASP283
A	ASP283

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Interaction with DNA substrate

Chain	Residue	Details
B	HIS309
A	HIS309

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
B	SER54
A	SER54

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694

Chain	Residue	Details
B	CYS65
B	CYS93
A	CYS65
A	CYS93

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
B	LYS197
A	LYS197

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352

Chain	Residue	Details
B	THR233
A	THR233

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17403694

Chain	Residue	Details
A	CYS310
B	CYS310

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 510

Chain	Residue	Details
A	ASP70	metal ligand
A	GLU96	metal ligand
A	TYR171	electrostatic stabiliser, metal ligand
A	ASP210	increase nucleophilicity, metal ligand, proton acceptor
A	ASN212
A	ASP283	electrostatic stabiliser
A	ASP308	metal ligand
A	HIS309	electrostatic stabiliser, metal ligand

---

site_id	MCSA2
Number of Residues	8
Details	M-CSA 510

Chain	Residue	Details
B	ASP70	metal ligand
B	GLU96	metal ligand
B	TYR171	electrostatic stabiliser, metal ligand
B	ASP210	increase nucleophilicity, metal ligand, proton acceptor
B	ASN212
B	ASP283	electrostatic stabiliser
B	ASP308	metal ligand
B	HIS309	electrostatic stabiliser, metal ligand

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