Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1TEZ

COMPLEX BETWEEN DNA AND THE DNA PHOTOLYASE FROM ANACYSTIS NIDULANS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003677	molecular_function	DNA binding
A	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006281	biological_process	DNA repair
A	0006950	biological_process	response to stress
A	0016829	molecular_function	lyase activity
A	0097159	molecular_function	organic cyclic compound binding
B	0000166	molecular_function	nucleotide binding
B	0003677	molecular_function	DNA binding
B	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006281	biological_process	DNA repair
B	0006950	biological_process	response to stress
B	0016829	molecular_function	lyase activity
B	0097159	molecular_function	organic cyclic compound binding
C	0000166	molecular_function	nucleotide binding
C	0003677	molecular_function	DNA binding
C	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006281	biological_process	DNA repair
C	0006950	biological_process	response to stress
C	0016829	molecular_function	lyase activity
C	0097159	molecular_function	organic cyclic compound binding
D	0000166	molecular_function	nucleotide binding
D	0003677	molecular_function	DNA binding
D	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006281	biological_process	DNA repair
D	0006950	biological_process	response to stress
D	0016829	molecular_function	lyase activity
D	0097159	molecular_function	organic cyclic compound binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 9001

Chain	Residue
B	ASP399
B	HOH9305
B	HOH9405
L	DC12
L	HOH1609

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 9002

Chain	Residue
J	HOH1610
J	HOH1611
A	ASP399
A	HOH9410
A	HOH9411
J	DC12

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE C I 13

Chain	Residue
A	ARG350
A	GLN411
I	TCP8
I	HOH1450
J	DG7
J	DA8

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE G I 14

Chain	Residue
A	ILE405
A	PHE406
A	ASN407
A	GLN411
J	DC6
J	DG7

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE C I 15

Chain	Residue
A	ASN407
A	GLN461

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE C K 13

Chain	Residue
B	ARG350
B	PHE406
B	GLN411
K	TCP8
K	HOH1407
L	DG7
L	DA8

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE G K 14

Chain	Residue
B	ILE405
B	PHE406
B	ASN407
B	GLN411
B	LYS414
L	DC6
L	DG7

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE C K 15

Chain	Residue
B	ASN407
B	GLN461

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD A 5485

Chain	Residue
A	TYR228
A	THR240
A	SER241
A	GLY242
A	LEU243
A	SER244
A	LEU247
A	TRP280
A	GLU283
A	ARG287
A	TYR290
A	TRP346
A	ASN349
A	ARG352
A	LEU378
A	ASP380
A	GLY381
A	ASP382
A	ALA385
A	ASN386
A	GLY389
A	TRP390
A	HOH9011
A	HOH9013
A	HOH9021
A	HOH9022
A	HOH9023
A	HOH9024
I	DT7
I	TCP8

site_id	BC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HDF A 5486

Chain	Residue
A	ARG10
A	PHE35
A	CYS36
A	LEU37
A	ASP38
A	ILE41
A	LEU42
A	MET47
A	ARG51
A	LEU55
A	ASP101
A	GLU103
A	GLY106
A	ARG109
A	LYS248
A	PHE249
A	HOH9003
A	HOH9102
A	HOH9112

site_id	BC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD B 6485

Chain	Residue
B	ARG287
B	TYR290
B	TRP346
B	ASN349
B	ARG352
B	LEU378
B	ASP380
B	GLY381
B	ASP382
B	ALA385
B	ASN386
B	GLY389
B	TRP390
B	HOH9010
B	HOH9012
B	HOH9020
B	HOH9021
B	HOH9022
B	HOH9023
K	DT7
K	TCP8
B	TYR228
B	THR240
B	SER241
B	GLY242
B	LEU243
B	SER244
B	LEU247
B	TRP280
B	GLU283

site_id	BC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HDF B 6486

Chain	Residue
B	ARG10
B	PHE35
B	CYS36
B	LEU37
B	ASP38
B	ILE41
B	LEU42
B	MET47
B	ARG51
B	LEU55
B	ASP101
B	GLU103
B	GLY106
B	ARG109
B	LYS248
B	PHE249
B	HOH9002
B	HOH9102
B	HOH9112

site_id	BC4
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD C 7485

Chain	Residue
C	TYR228
C	THR240
C	SER241
C	GLY242
C	LEU243
C	SER244
C	LEU247
C	TRP280
C	GLU283
C	ARG287
C	TYR290
C	TRP346
C	ASN349
C	ARG352
C	LEU378
C	ASP380
C	GLY381
C	ASP382
C	ALA385
C	ASN386
C	GLY389
C	TRP390
C	HOH7496
C	HOH7498
C	HOH7506
C	HOH7508
C	HOH7509
C	HOH7510
C	HOH7836

site_id	BC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HDF C 7486

Chain	Residue
C	ARG10
C	PHE35
C	CYS36
C	LEU37
C	ASP38
C	ILE41
C	LEU42
C	MET47
C	ARG51
C	LEU55
C	ASP101
C	GLU103
C	GLY106
C	ARG109
C	LYS248
C	PHE249
C	HOH7488
C	HOH7589
C	HOH7599

site_id	BC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD D 8485

Chain	Residue
D	TYR228
D	THR240
D	SER241
D	GLY242
D	LEU243
D	SER244
D	LEU247
D	TRP280
D	GLU283
D	ARG287
D	TYR290
D	TRP346
D	MET347
D	ASN349
D	ARG352
D	LEU378
D	ASP380
D	GLY381
D	ASP382
D	ALA385
D	ASN386
D	GLY389
D	TRP390
D	HOH8496
D	HOH8498
D	HOH8506
D	HOH8508
D	HOH8509
D	HOH8510

site_id	BC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HDF D 8486

Chain	Residue
D	ARG10
D	PHE35
D	CYS36
D	LEU37
D	ASP38
D	ILE41
D	LEU42
D	MET47
D	ARG51
D	LEU55
D	ASP101
D	GLU103
D	GLY106
D	ARG109
D	LYS248
D	PHE249
D	HOH8488
D	HOH8588
D	HOH8598

Functional Information from PROSITE/UniProt

site_id	PS00394
Number of Residues	13
Details	DNA_PHOTOLYASES_1_1 DNA photolyases class 1 signature 1. TGyPIVDAaMRqL

Chain	Residue	Details
A	THR329-LEU341

site_id	PS00691
Number of Residues	20
Details	DNA_PHOTOLYASES_1_2 DNA photolyases class 1 signature 2. NRcRMIvASFLtKdLiidWR

Chain	Residue	Details
A	ASN349-ARG368

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	BINDING:

Chain	Residue	Details
A	CYS36
B	ASP101
B	ARG232
B	LYS248
B	GLN411
B	LYS472
C	CYS36
C	ARG51
C	ASP101
C	ARG232
C	LYS248
A	ARG51
C	GLN411
C	LYS472
D	CYS36
D	ARG51
D	ASP101
D	ARG232
D	LYS248
D	GLN411
D	LYS472
A	ASP101
A	ARG232
A	LYS248
A	GLN411
A	LYS472
B	CYS36
B	ARG51

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:15213381, ECO:0000269\|PubMed:15576622, ECO:0000269\|PubMed:9360600

Chain	Residue	Details
A	TYR228
B	ASN386
C	TYR228
C	THR240
C	TRP346
C	ASP380
C	ASN386
D	TYR228
D	THR240
D	TRP346
D	ASP380
A	THR240
D	ASN386
A	TRP346
A	ASP380
A	ASN386
B	TYR228
B	THR240
B	TRP346
B	ASP380

site_id	SWS_FT_FI3
Number of Residues	12
Details	SITE: Electron transfer via tryptophanyl radical => ECO:0000250

Chain	Residue	Details
A	TRP314
D	TRP314
D	TRP367
D	TRP390
A	TRP367
A	TRP390
B	TRP314
B	TRP367
B	TRP390
C	TRP314
C	TRP367
C	TRP390

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
A	TRP314
A	TRP390
A	TRP367

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
B	TRP314
B	TRP390
B	TRP367

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
C	TRP314
C	TRP390
C	TRP367

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
D	TRP314
D	TRP390
D	TRP367

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)