Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4JAY

Crystal structure of P. aeruginosa MurB in complex with NADP+

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD A 1001

Chain	Residue
A	VAL51
A	PRO118
A	GLY119
A	THR120
A	ALA123
A	MET126
A	GLN127
A	ILE129
A	GLY130
A	ALA131
A	TRP177
A	GLY53
A	ILE179
A	ARG224
A	ASN236
A	GLY238
A	ASN337
A	NAP1002
A	HOH1104
A	HOH1111
A	HOH1123
A	HOH1130
A	GLY54
A	HOH1150
A	GLY55
A	SER56
A	ASN57
A	LEU58
A	MET71
A	ILE117

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAP A 1002

Chain	Residue
A	ALA131
A	TYR132
A	ARG166
A	ASP195
A	TYR196
A	LYS227
A	GLY238
A	SER239
A	ASN243
A	TYR264
A	LYS272
A	GLU335
A	FAD1001
A	K1004
A	HOH1139
A	HOH1143
A	HOH1157

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE B3P A 1003

Chain	Residue
A	GLY133
A	VAL134
A	GLU135
A	ASP138
A	HIS193
A	ASP195
A	HOH1153
A	HOH1171
C	GLY282
C	GLY283
C	TRP284
C	PHE287
C	ARG319

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 1004

Chain	Residue
A	ASN57
A	ALA237
A	SER239
A	GLU335
A	NAP1002

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 401

Chain	Residue
B	ASN57
B	ALA237
B	SER239
B	GLU335
B	FAD402
B	NAP403

site_id	AC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD B 402

Chain	Residue
B	HOH528
B	HOH532
B	VAL51
B	GLY53
B	GLY54
B	GLY55
B	SER56
B	ASN57
B	LEU58
B	MET71
B	ILE117
B	PRO118
B	GLY119
B	THR120
B	ALA123
B	MET126
B	GLN127
B	ILE129
B	GLY130
B	ALA131
B	TRP177
B	ILE179
B	ARG224
B	ASN236
B	ALA237
B	GLY238
B	ASN337
B	K401
B	NAP403
B	HOH505

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAP B 403

Chain	Residue
B	ALA131
B	TYR132
B	TYR165
B	ARG166
B	TYR196
B	LYS227
B	LEU228
B	GLY238
B	SER239
B	ASN243
B	TYR264
B	LYS272
B	GLN298
B	GLU335
B	K401
B	FAD402
B	HOH562
B	HOH568

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE B3P B 404

Chain	Residue
A	GLY282
A	GLY283
A	TRP284
A	PHE287
B	GLY133
B	VAL134
B	GLU135
B	ASP138
B	HIS193
B	ASP195
B	HOH544

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 401

Chain	Residue
C	ASN57
C	ALA237
C	SER239
C	GLU335
C	FAD402
C	NAP403

site_id	BC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD C 402

Chain	Residue
C	VAL51
C	ILE52
C	GLY53
C	GLY54
C	GLY55
C	SER56
C	ASN57
C	LEU58
C	MET71
C	ILE117
C	PRO118
C	GLY119
C	THR120
C	ALA123
C	MET126
C	GLN127
C	ILE129
C	GLY130
C	ALA131
C	TRP177
C	ILE179
C	ARG224
C	ASN236
C	ALA237
C	GLY238
C	ASN337
C	K401
C	NAP403
C	HOH501
C	HOH505
C	HOH527
C	HOH576

site_id	BC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAP C 403

Chain	Residue
C	ALA131
C	TYR132
C	ARG166
C	TYR196
C	LYS227
C	GLY238
C	SER239
C	ASN243
C	TYR264
C	LYS272
C	GLN298
C	GLU335
C	K401
C	FAD402
C	HOH524
C	HOH528
C	HOH536
C	HOH547

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE B3P C 404

Chain	Residue
C	GLY133
C	VAL134
C	ASP138
C	HIS193
C	ASP195
C	HOH548
D	GLY282
D	TRP284
D	PHE287
D	ARG319

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 401

Chain	Residue
D	ASN57
D	ALA237
D	SER239
D	GLU335
D	FAD402
D	NAP403

site_id	BC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD D 402

Chain	Residue
D	VAL51
D	ILE52
D	GLY53
D	GLY54
D	GLY55
D	SER56
D	ASN57
D	LEU58
D	MET71
D	ILE117
D	PRO118
D	GLY119
D	THR120
D	ALA123
D	MET126
D	GLN127
D	ILE129
D	GLY130
D	ALA131
D	TRP177
D	ILE179
D	ARG224
D	ASN236
D	ALA237
D	GLY238
D	ASN337
D	K401
D	NAP403
D	HOH503
D	HOH508
D	HOH518
D	HOH566

site_id	BC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAP D 403

Chain	Residue
D	ALA131
D	TYR132
D	ARG166
D	ASP195
D	TYR196
D	LYS227
D	GLY238
D	SER239
D	ASN243
D	TYR264
D	LYS272
D	GLU335
D	K401
D	FAD402
D	HOH532
D	HOH533
D	HOH545
D	HOH558
D	HOH561

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE B3P D 404

Chain	Residue
B	GLY282
B	GLY283
B	TRP284
B	PHE287
D	GLY133
D	VAL134
D	GLU135
D	ASP138
D	HIS193
D	ASP195
D	HOH569

Functional Information from PROSITE/UniProt

site_id	PS00430
Number of Residues	92
Details	TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. smslelqehcslkpyntfgidvrarllahardeadvrealalarerglpllvigggsnllltrdvealvlrmasqgrrivsdaa...............................DSVLVEAE

Chain	Residue	Details
A	SER0-GLU91

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	684
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00037","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00037","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00037","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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