2O3H

Crystal structure of the human C65A Ape

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SM A 400

Chain	Residue
A	GLU216
A	GLU217
A	GLU242
A	GLN245
A	HOH506
A	HOH589
A	HOH646

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SM A 401

Chain	Residue
A	HOH559
A	HOH593
A	HOH676
A	HOH703
A	HOH789
A	ASP70
A	GLU96

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT A 500

Chain	Residue
A	LYS78
A	LEU104
A	ALA106
A	GLN109
A	HOH652
A	HOH697
A	HOH784

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 501

Chain	Residue
A	ASN272
A	ARG274
A	SER275

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT A 502

Chain	Residue
A	MET37
A	ALA38
A	SER120
A	TYR144
A	ASP152
A	HOH523
A	HOH530

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT A 503

Chain	Residue
A	SER56
A	TYR128
A	SER129
A	TYR171

---

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	1
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15380100

Chain	Residue	Details
A	VAL172

---

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

Chain	Residue	Details
A	LEU211

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764

Chain	Residue	Details
A	CYS310

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00764

Chain	Residue	Details
A	VAL69
A	THR97
A	LEU211
A	VAL213
A	HIS309
A	CYS310

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:8932375

Chain	Residue	Details
A	VAL213

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799

Chain	Residue	Details
A	TYR284

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Interaction with DNA substrate

Chain	Residue	Details
A	CYS310

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	PRO55

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694

Chain	Residue	Details
A	SER66
A	LEU94

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	GLY198

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352

Chain	Residue	Details
A	PRO234

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17403694

Chain	Residue	Details
A	PRO311

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 510

Chain	Residue	Details
A	GLY71	metal ligand
A	THR97	metal ligand
A	VAL172	electrostatic stabiliser, metal ligand
A	LEU211	increase nucleophilicity, metal ligand, proton acceptor
A	VAL213
A	TYR284	electrostatic stabiliser
A	HIS309	metal ligand
A	CYS310	electrostatic stabiliser, metal ligand

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