Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3T1I

Crystal Structure of Human Mre11: Understanding Tumorigenic Mutations

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004519	molecular_function	endonuclease activity
A	0004520	molecular_function	DNA endonuclease activity
A	0005634	cellular_component	nucleus
A	0006302	biological_process	double-strand break repair
A	0008296	molecular_function	3'-5'-DNA exonuclease activity
A	0016787	molecular_function	hydrolase activity
A	0030145	molecular_function	manganese ion binding
A	0030870	cellular_component	Mre11 complex
B	0004519	molecular_function	endonuclease activity
B	0004520	molecular_function	DNA endonuclease activity
B	0005634	cellular_component	nucleus
B	0006302	biological_process	double-strand break repair
B	0008296	molecular_function	3'-5'-DNA exonuclease activity
B	0016787	molecular_function	hydrolase activity
B	0030145	molecular_function	manganese ion binding
B	0030870	cellular_component	Mre11 complex
C	0004519	molecular_function	endonuclease activity
C	0004520	molecular_function	DNA endonuclease activity
C	0005634	cellular_component	nucleus
C	0006302	biological_process	double-strand break repair
C	0008296	molecular_function	3'-5'-DNA exonuclease activity
C	0016787	molecular_function	hydrolase activity
C	0030145	molecular_function	manganese ion binding
C	0030870	cellular_component	Mre11 complex
D	0004519	molecular_function	endonuclease activity
D	0004520	molecular_function	DNA endonuclease activity
D	0005634	cellular_component	nucleus
D	0006302	biological_process	double-strand break repair
D	0008296	molecular_function	3'-5'-DNA exonuclease activity
D	0016787	molecular_function	hydrolase activity
D	0030145	molecular_function	manganese ion binding
D	0030870	cellular_component	Mre11 complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 412

Chain	Residue
A	ASP20
A	HIS22
A	ASP60
A	HIS247
A	MN413
A	HOH504
A	HOH519

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 413

Chain	Residue
A	HIS217
A	HIS245
A	MN412
A	HOH519
A	ASP60
A	ASN128

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DTT A 451

Chain	Residue
A	ARG69
A	GOL453

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DTT A 452

Chain	Residue
A	LYS250
A	ILE251
A	ALA252
A	HIS283
A	LYS298

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 453

Chain	Residue
A	CYS146
A	DTT451

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 454

Chain	Residue
A	ASN128
A	HIS129
A	HOH518

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 455

Chain	Residue
A	PHE37
A	HOH513

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 456

Chain	Residue
A	PHE193
A	LYS196
A	PHE233

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 457

Chain	Residue
A	HIS302
A	GLY353
A	HIS356

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 458

Chain	Residue
A	GLN90
A	GLU92

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 412

Chain	Residue
B	ASP20
B	HIS22
B	ASP60
B	HIS247
B	MN413
B	HOH507

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 413

Chain	Residue
B	ASP60
B	ASN128
B	HIS217
B	HIS245
B	MN412
B	HOH507

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN C 412

Chain	Residue
C	ASP20
C	HIS22
C	ASP60
C	HIS247
C	MN413
C	HOH509
C	HOH520

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN C 413

Chain	Residue
C	ASP60
C	ASN128
C	HIS217
C	HIS245
C	MN412
C	HOH509

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 451

Chain	Residue
C	SER98
C	SER145
C	GLY148
C	VAL150

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 452

Chain	Residue
C	PHE193
C	VAL194
C	LYS196
C	PHE233

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 453

Chain	Residue
C	GLU278
C	ALA279
C	VAL280
C	GLN306
C	PHE307

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 454

Chain	Residue
C	SER145
C	CYS146
C	HOH508

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 455

Chain	Residue
C	MSE26
C	ARG32
C	THR272
C	LEU274

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 456

Chain	Residue
C	ASN219
C	HIS245
C	GLU246
C	HIS247
C	HOH506

site_id	CC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN D 412

Chain	Residue
D	ASP20
D	HIS22
D	ASP60
D	HIS247
D	MN413
D	HOH504
D	HOH508

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN D 413

Chain	Residue
D	ASP20
D	ASP60
D	ASN128
D	HIS217
D	HIS245
D	MN412
D	HOH504

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL D 451

Chain	Residue
D	ASN128

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 452

Chain	Residue
D	PRO166
D	LEU168
D	LYS204

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 453

Chain	Residue
D	ASN34
D	LEU78

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	HIS129
B	HIS129
C	HIS129
D	HIS129

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q61216

Chain	Residue	Details
A	SER2
B	SER2
C	SER2
D	SER2

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER275
B	SER275
C	SER275
D	SER275

site_id	SWS_FT_FI4
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS255
B	LYS255
C	LYS255
D	LYS255

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