Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4AD9

Crystal structure of human LACTB2.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003727	molecular_function	single-stranded RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0090502	biological_process	obsolete RNA phosphodiester bond hydrolysis, endonucleolytic
B	0003723	molecular_function	RNA binding
B	0003727	molecular_function	single-stranded RNA binding
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0090502	biological_process	obsolete RNA phosphodiester bond hydrolysis, endonucleolytic
C	0003723	molecular_function	RNA binding
C	0003727	molecular_function	single-stranded RNA binding
C	0004518	molecular_function	nuclease activity
C	0004519	molecular_function	endonuclease activity
C	0004521	molecular_function	RNA endonuclease activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0090502	biological_process	obsolete RNA phosphodiester bond hydrolysis, endonucleolytic
D	0003723	molecular_function	RNA binding
D	0003727	molecular_function	single-stranded RNA binding
D	0004518	molecular_function	nuclease activity
D	0004519	molecular_function	endonuclease activity
D	0004521	molecular_function	RNA endonuclease activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0008270	molecular_function	zinc ion binding
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0090502	biological_process	obsolete RNA phosphodiester bond hydrolysis, endonucleolytic
E	0003723	molecular_function	RNA binding
E	0003727	molecular_function	single-stranded RNA binding
E	0004518	molecular_function	nuclease activity
E	0004519	molecular_function	endonuclease activity
E	0004521	molecular_function	RNA endonuclease activity
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0008270	molecular_function	zinc ion binding
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
E	0090502	biological_process	obsolete RNA phosphodiester bond hydrolysis, endonucleolytic
F	0003723	molecular_function	RNA binding
F	0003727	molecular_function	single-stranded RNA binding
F	0004518	molecular_function	nuclease activity
F	0004519	molecular_function	endonuclease activity
F	0004521	molecular_function	RNA endonuclease activity
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0008270	molecular_function	zinc ion binding
F	0016787	molecular_function	hydrolase activity
F	0046872	molecular_function	metal ion binding
F	0090502	biological_process	obsolete RNA phosphodiester bond hydrolysis, endonucleolytic

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 1000

Chain	Residue
A	ASP81
A	HIS82
A	ASP164
A	HIS199
A	ZN1001
A	HOH2042
A	HOH2083

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 1001

Chain	Residue
A	HIS145
A	ASP164
A	ZN1000
A	HOH2083
C	GLU118
A	HIS77
A	HIS79

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 1000

Chain	Residue
A	HOH2130
B	ASP81
B	HIS82
B	ASP164
B	HIS199
B	ZN1001

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN B 1001

Chain	Residue
A	GLU118
A	HOH2130
B	HIS77
B	HIS79
B	HIS145
B	ASP164
B	ZN1000

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN C 1000

Chain	Residue
B	GLU118
B	HOH2064
C	ASP81
C	HIS82
C	ASP164
C	HIS199
C	ZN1001

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN C 1001

Chain	Residue
B	GLU118
B	HOH2064
C	HIS77
C	HIS79
C	HIS145
C	ASP164
C	ZN1000

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN D 1000

Chain	Residue
D	ASP81
D	HIS82
D	ASP164
D	HIS199
D	ZN1001
D	HOH2031
D	HOH2060

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN D 1001

Chain	Residue
D	HIS77
D	HIS79
D	HIS145
D	ASP164
D	ZN1000
D	HOH2060
F	GLU118

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN E 1001

Chain	Residue
D	GLU118
D	HOH2099
E	HIS77
E	HIS79
E	HIS145
E	ASP164
E	ZN1000

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ZN F 1000

Chain	Residue
E	GLU118
E	HOH2066
E	HOH2067
F	ASP81
F	HIS82
F	ASP164
F	HIS199
F	ZN1001

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN F 1001

Chain	Residue
E	GLU118
E	HOH2067
F	HIS77
F	HIS79
F	HIS145
F	ASP164
F	ZN1000

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO F 1289

Chain	Residue
F	HIS216
F	ARG217
F	ARG220
F	ASN260
F	HIS264

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1289

Chain	Residue
A	HIS216
A	ARG217
A	ARG220
A	ASN260
A	HIS264

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO D 1289

Chain	Residue
D	LYS266
D	GLU269

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 1290

Chain	Residue
D	HIS216
D	ARG217
D	ARG220
D	ASN260
D	HIS264

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PDB","id":"4AD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99KR3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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