Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5JZX

Crystal Structure of UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) from Mycobacterium tuberculosis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008360	biological_process	regulation of cell shape
A	0008762	molecular_function	UDP-N-acetylmuramate dehydrogenase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization
A	0071949	molecular_function	FAD binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008360	biological_process	regulation of cell shape
B	0008762	molecular_function	UDP-N-acetylmuramate dehydrogenase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051301	biological_process	cell division
B	0071555	biological_process	cell wall organization
B	0071949	molecular_function	FAD binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008360	biological_process	regulation of cell shape
C	0008762	molecular_function	UDP-N-acetylmuramate dehydrogenase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0051301	biological_process	cell division
C	0071555	biological_process	cell wall organization
C	0071949	molecular_function	FAD binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008360	biological_process	regulation of cell shape
D	0008762	molecular_function	UDP-N-acetylmuramate dehydrogenase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0051301	biological_process	cell division
D	0071555	biological_process	cell wall organization
D	0071949	molecular_function	FAD binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0008360	biological_process	regulation of cell shape
E	0008762	molecular_function	UDP-N-acetylmuramate dehydrogenase activity
E	0009252	biological_process	peptidoglycan biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0051301	biological_process	cell division
E	0071555	biological_process	cell wall organization
E	0071949	molecular_function	FAD binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0008360	biological_process	regulation of cell shape
F	0008762	molecular_function	UDP-N-acetylmuramate dehydrogenase activity
F	0009252	biological_process	peptidoglycan biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0050660	molecular_function	flavin adenine dinucleotide binding
F	0051301	biological_process	cell division
F	0071555	biological_process	cell wall organization
F	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	34
Details	binding site for residue FAD A 401

Chain	Residue
A	THR26
A	ILE127
A	PRO128
A	GLY129
A	SER130
A	ALA133
A	VAL136
A	VAL139
A	GLY140
A	ALA141
A	ARG176
A	VAL65
A	GLY185
A	VAL188
A	VAL191
A	VAL192
A	ARG238
A	SER254
A	VAL255
A	GLY256
A	K402
A	HOH527
A	ALA67
A	HOH548
A	HOH549
A	HOH555
A	HOH592
A	HOH593
A	GLY68
A	GLY69
A	SER70
A	ASN71
A	LEU72
A	LEU86

site_id	AC2
Number of Residues	5
Details	binding site for residue K A 402

Chain	Residue
A	ASN71
A	VAL255
A	SER257
A	GLU361
A	FAD401

site_id	AC3
Number of Residues	29
Details	binding site for residue FAD B 401

Chain	Residue
B	THR26
B	PHE66
B	ALA67
B	GLY68
B	GLY69
B	SER70
B	ASN71
B	LEU86
B	ILE127
B	PRO128
B	GLY129
B	SER130
B	ALA133
B	VAL136
B	VAL139
B	GLY140
B	ALA141
B	THR190
B	VAL191
B	VAL192
B	ARG238
B	SER254
B	VAL255
B	GLY256
B	VAL363
B	K402
B	HOH510
B	HOH516
B	HOH522

site_id	AC4
Number of Residues	2
Details	binding site for residue K B 402

Chain	Residue
B	GLN137
B	FAD401

site_id	AC5
Number of Residues	34
Details	binding site for residue FAD C 401

Chain	Residue
C	HOH501
C	HOH511
C	HOH544
C	HOH560
C	HOH562
C	THR26
C	VAL65
C	PHE66
C	ALA67
C	GLY68
C	GLY69
C	SER70
C	ASN71
C	LEU86
C	ILE127
C	PRO128
C	GLY129
C	SER130
C	GLY132
C	ALA133
C	VAL136
C	GLN137
C	VAL139
C	GLY140
C	ALA141
C	ARG176
C	THR190
C	VAL191
C	VAL192
C	ARG238
C	SER254
C	VAL255
C	GLY256
C	VAL363

site_id	AC6
Number of Residues	4
Details	binding site for residue K C 402

Chain	Residue
C	VAL255
C	SER257
C	GLU361
C	HOH567

site_id	AC7
Number of Residues	32
Details	binding site for residue FAD D 401

Chain	Residue
D	THR26
D	VAL65
D	ALA67
D	GLY68
D	GLY69
D	SER70
D	ASN71
D	LEU86
D	ILE127
D	PRO128
D	GLY129
D	SER130
D	GLY132
D	ALA133
D	VAL136
D	GLN137
D	VAL139
D	GLY140
D	ALA141
D	ARG176
D	THR190
D	VAL191
D	VAL192
D	ARG238
D	SER254
D	VAL255
D	GLY256
D	HOH509
D	HOH528
D	HOH548
D	HOH562
D	HOH570

site_id	AC8
Number of Residues	28
Details	binding site for residue FAD E 401

Chain	Residue
E	THR26
E	VAL65
E	PHE66
E	ALA67
E	GLY68
E	GLY69
E	SER70
E	ASN71
E	LEU86
E	PRO128
E	GLY129
E	SER130
E	ALA133
E	VAL136
E	VAL139
E	GLY140
E	ALA141
E	ARG176
E	VAL188
E	THR190
E	VAL191
E	VAL192
E	ARG238
E	MET243
E	SER254
E	VAL255
E	GLY256
E	HOH509

site_id	AC9
Number of Residues	30
Details	binding site for residue FAD F 401

Chain	Residue
F	THR26
F	VAL65
F	PHE66
F	ALA67
F	GLY68
F	GLY69
F	SER70
F	ASN71
F	LEU72
F	LEU86
F	ILE127
F	PRO128
F	SER130
F	GLY132
F	ALA133
F	VAL136
F	VAL139
F	GLY140
F	ALA141
F	ARG176
F	GLY185
F	VAL188
F	THR190
F	VAL191
F	VAL192
F	ARG238
F	MET243
F	SER254
F	VAL255
F	GLY256

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	173
Details	Domain: {"description":"FAD-binding PCMH-type"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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