Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1BIX

THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000723	biological_process	telomere maintenance
A	0000781	cellular_component	chromosome, telomeric region
A	0003677	molecular_function	DNA binding
A	0003684	molecular_function	damaged DNA binding
A	0003691	molecular_function	double-stranded telomeric DNA binding
A	0003713	molecular_function	transcription coactivator activity
A	0003714	molecular_function	transcription corepressor activity
A	0003723	molecular_function	RNA binding
A	0003824	molecular_function	catalytic activity
A	0003906	molecular_function	DNA-(apurinic or apyrimidinic site) endonuclease activity
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004520	molecular_function	DNA endonuclease activity
A	0004523	molecular_function	RNA-DNA hybrid ribonuclease activity
A	0004527	molecular_function	exonuclease activity
A	0004528	molecular_function	phosphodiesterase I activity
A	0004844	molecular_function	uracil DNA N-glycosylase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005783	cellular_component	endoplasmic reticulum
A	0005813	cellular_component	centrosome
A	0005840	cellular_component	ribosome
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0006287	biological_process	base-excision repair, gap-filling
A	0006308	biological_process	DNA catabolic process
A	0006310	biological_process	DNA recombination
A	0006974	biological_process	DNA damage response
A	0008081	molecular_function	phosphoric diester hydrolase activity
A	0008296	molecular_function	3'-5'-DNA exonuclease activity
A	0008309	molecular_function	double-stranded DNA exodeoxyribonuclease activity
A	0008311	molecular_function	double-stranded DNA 3'-5' DNA exonuclease activity
A	0008408	molecular_function	3'-5' exonuclease activity
A	0016491	molecular_function	oxidoreductase activity
A	0016607	cellular_component	nuclear speck
A	0016787	molecular_function	hydrolase activity
A	0031490	molecular_function	chromatin DNA binding
A	0033892	molecular_function	deoxyribonuclease (pyrimidine dimer) activity
A	0042981	biological_process	regulation of apoptotic process
A	0043488	biological_process	regulation of mRNA stability
A	0044029	biological_process	positive regulation of gene expression via chromosomal CpG island demethylation
A	0045454	biological_process	cell redox homeostasis
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0052720	molecular_function	class II DNA-(apurinic or apyrimidinic site) endonuclease activity
A	0090580	molecular_function	phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands
A	0097698	biological_process	telomere maintenance via base-excision repair
A	0140431	molecular_function	DNA-(abasic site) binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SM A 400

Chain	Residue
A	GLU216
A	GLU217
A	GLU242
A	GLN245
A	HOH566

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SM A 401

Chain	Residue
A	ASP70
A	GLU96
A	HOH563

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SM A 402

Chain	Residue
A	GLU46
A	ASP148
A	GLU150

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SM A 403

Chain	Residue
A	ASP124
A	GLU126
A	LEU318

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PT A 404

Chain	Residue
A	MET271
A	LYS276

site_id	ROX
Number of Residues	1
Details	CYS 65 HAS BEEN PROPOSED TO BE INVOLVED IN THE REDUCTIVE ACTIVATION OF A NUMBER OF TRANSCRIPTION FACTORS INCLUDING FOS/JUN AND P53.

Chain	Residue
A	CYS65

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	29
Details	Region: {"description":"Mitochondrial targeting sequence (MTS)"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Motif: {"description":"Nuclear export signal (NES)"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"15380100","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9351835","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BIX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8932375","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"21762700","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9804799","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Site: {"description":"Interaction with DNA substrate"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CDK5","evidences":[{"source":"UniProtKB","id":"P28352","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 12758078, 10390343, 15380100, 10871340

Chain	Residue	Details
A	HIS309
A	ASP283
A	ASP210
A	TYR171

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)