Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5Z2L

Crystal structure of BdcA in complex with NADPH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0035438	molecular_function	cyclic-di-GMP binding
A	0042803	molecular_function	protein homodimerization activity
A	0044010	biological_process	single-species biofilm formation
A	0070402	molecular_function	NADPH binding
B	0035438	molecular_function	cyclic-di-GMP binding
B	0042803	molecular_function	protein homodimerization activity
B	0044010	biological_process	single-species biofilm formation
B	0070402	molecular_function	NADPH binding
C	0035438	molecular_function	cyclic-di-GMP binding
C	0042803	molecular_function	protein homodimerization activity
C	0044010	biological_process	single-species biofilm formation
C	0070402	molecular_function	NADPH binding
D	0035438	molecular_function	cyclic-di-GMP binding
D	0042803	molecular_function	protein homodimerization activity
D	0044010	biological_process	single-species biofilm formation
D	0070402	molecular_function	NADPH binding
E	0035438	molecular_function	cyclic-di-GMP binding
E	0042803	molecular_function	protein homodimerization activity
E	0044010	biological_process	single-species biofilm formation
E	0070402	molecular_function	NADPH binding
F	0035438	molecular_function	cyclic-di-GMP binding
F	0042803	molecular_function	protein homodimerization activity
F	0044010	biological_process	single-species biofilm formation
F	0070402	molecular_function	NADPH binding
G	0035438	molecular_function	cyclic-di-GMP binding
G	0042803	molecular_function	protein homodimerization activity
G	0044010	biological_process	single-species biofilm formation
G	0070402	molecular_function	NADPH binding
H	0035438	molecular_function	cyclic-di-GMP binding
H	0042803	molecular_function	protein homodimerization activity
H	0044010	biological_process	single-species biofilm formation
H	0070402	molecular_function	NADPH binding
I	0035438	molecular_function	cyclic-di-GMP binding
I	0042803	molecular_function	protein homodimerization activity
I	0044010	biological_process	single-species biofilm formation
I	0070402	molecular_function	NADPH binding
J	0035438	molecular_function	cyclic-di-GMP binding
J	0042803	molecular_function	protein homodimerization activity
J	0044010	biological_process	single-species biofilm formation
J	0070402	molecular_function	NADPH binding
K	0035438	molecular_function	cyclic-di-GMP binding
K	0042803	molecular_function	protein homodimerization activity
K	0044010	biological_process	single-species biofilm formation
K	0070402	molecular_function	NADPH binding
L	0035438	molecular_function	cyclic-di-GMP binding
L	0042803	molecular_function	protein homodimerization activity
L	0044010	biological_process	single-species biofilm formation
L	0070402	molecular_function	NADPH binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue PG0 A 301

Chain	Residue
A	GLY89
A	ALA141
C	HIS240
C	HIS242

site_id	AC2
Number of Residues	33
Details	binding site for residue NDP A 302

Chain	Residue
A	ALA38
A	GLY39
A	SER40
A	THR58
A	ASP59
A	SER60
A	ASN82
A	ALA83
A	GLY84
A	ILE85
A	ILE105
A	ILE130
A	GLY131
A	SER132
A	TYR146
A	LYS150
A	PRO176
A	GLY177
A	PRO178
A	ILE179
A	THR181
A	ALA183
A	ASN184
A	HOH406
A	HOH421
A	HOH446
A	HOH454
A	HOH473
A	SER15
A	ARG16
A	GLY17
A	ILE18
A	TYR37

site_id	AC3
Number of Residues	35
Details	binding site for residue NDP D 301

Chain	Residue
D	SER15
D	ARG16
D	GLY17
D	ILE18
D	TYR37
D	ALA38
D	GLY39
D	SER40
D	THR58
D	ASP59
D	SER60
D	ASN82
D	ALA83
D	GLY84
D	ILE85
D	ILE105
D	ILE130
D	GLY131
D	SER132
D	TYR146
D	LYS150
D	PRO176
D	GLY177
D	PRO178
D	ILE179
D	THR181
D	ALA183
D	ASN184
D	HOH424
D	HOH431
D	HOH432
D	HOH433
D	HOH487
D	HOH509
D	HOH536

site_id	AC4
Number of Residues	8
Details	binding site for residue EDO B 301

Chain	Residue
B	VAL140
B	MET143
B	MET193
B	LEU197
B	PHE235
B	HOH415
B	HOH457
D	HOH500

site_id	AC5
Number of Residues	34
Details	binding site for residue NDP B 302

Chain	Residue
B	LYS150
B	PRO176
B	GLY177
B	PRO178
B	ILE179
B	THR181
B	ALA183
B	ASN184
B	HOH405
B	HOH411
B	HOH424
B	HOH478
B	HOH486
B	HOH514
B	HOH532
B	SER15
B	ARG16
B	GLY17
B	ILE18
B	TYR37
B	ALA38
B	GLY39
B	SER40
B	THR58
B	ASP59
B	SER60
B	ASN82
B	ALA83
B	GLY84
B	ILE105
B	ILE130
B	GLY131
B	SER132
B	TYR146

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL C 301

Chain	Residue
C	VAL133
C	ASN134
C	PRO176
C	GLY177
C	ASN184
C	PHE235
C	NDP304

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO C 302

Chain	Residue
C	ALA61
C	ASP62
C	LYS104

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO C 303

Chain	Residue
C	ASP62
C	ARG63
C	ASP64
C	HOH401
C	HOH414

site_id	AC9
Number of Residues	35
Details	binding site for residue NDP C 304

Chain	Residue
C	SER15
C	ARG16
C	GLY17
C	ILE18
C	TYR37
C	ALA38
C	GLY39
C	SER40
C	THR58
C	ASP59
C	SER60
C	ASN82
C	ALA83
C	GLY84
C	ILE105
C	ILE130
C	GLY131
C	SER132
C	TYR146
C	LYS150
C	PRO176
C	GLY177
C	PRO178
C	ILE179
C	THR181
C	ALA183
C	ASN184
C	GOL301
C	HOH428
C	HOH431
C	HOH433
C	HOH451
C	HOH483
C	HOH494
C	HOH561

site_id	AD1
Number of Residues	4
Details	binding site for residue GOL E 301

Chain	Residue
E	TYR146
E	ALA183
E	NDP303
E	HOH418

site_id	AD2
Number of Residues	36
Details	binding site for residue NDP E 303

Chain	Residue
E	GLY13
E	SER15
E	ARG16
E	GLY17
E	ILE18
E	TYR37
E	ALA38
E	GLY39
E	SER40
E	THR58
E	ASP59
E	SER60
E	ASN82
E	ALA83
E	GLY84
E	ILE85
E	ILE105
E	ILE130
E	GLY131
E	SER132
E	TYR146
E	LYS150
E	PRO176
E	GLY177
E	PRO178
E	ILE179
E	THR181
E	ALA183
E	ASN184
E	GOL301
E	HOH411
E	HOH435
E	HOH439
E	HOH448
E	HOH458
E	HOH511

site_id	AD3
Number of Residues	36
Details	binding site for residue NDP J 301

Chain	Residue
J	GLY13
J	SER15
J	ARG16
J	GLY17
J	ILE18
J	TYR37
J	ALA38
J	GLY39
J	SER40
J	THR58
J	ASP59
J	SER60
J	ASN82
J	ALA83
J	GLY84
J	ILE85
J	ILE105
J	ILE130
J	GLY131
J	SER132
J	TYR146
J	LYS150
J	PRO176
J	GLY177
J	PRO178
J	ILE179
J	THR181
J	ALA183
J	ASN184
J	HOH423
J	HOH424
J	HOH432
J	HOH439
J	HOH441
J	HOH450
J	HOH494

site_id	AD4
Number of Residues	31
Details	binding site for residue NDP H 301

Chain	Residue
H	SER15
H	ARG16
H	GLY17
H	ILE18
H	TYR37
H	ALA38
H	GLY39
H	SER40
H	THR58
H	ASP59
H	SER60
H	ASN82
H	ALA83
H	GLY84
H	ILE85
H	ILE105
H	ILE130
H	GLY131
H	SER132
H	TYR146
H	LYS150
H	PRO176
H	GLY177
H	PRO178
H	ILE179
H	THR181
H	ALA183
H	ASN184
H	HOH403
H	HOH404
H	HOH454

site_id	AD5
Number of Residues	7
Details	binding site for residue PEG K 301

Chain	Residue
K	ARG202
K	GLU207
K	GLU208
K	HOH496
L	ARG24
L	GLU50
L	HOH420

site_id	AD6
Number of Residues	35
Details	binding site for residue NDP K 302

Chain	Residue
K	GLY13
K	SER15
K	ARG16
K	GLY17
K	ILE18
K	TYR37
K	ALA38
K	GLY39
K	SER40
K	THR58
K	ASP59
K	SER60
K	ASN82
K	ALA83
K	GLY84
K	ILE105
K	ILE130
K	GLY131
K	SER132
K	TYR146
K	LYS150
K	PRO176
K	GLY177
K	PRO178
K	ILE179
K	THR181
K	ALA183
K	ASN184
K	HOH408
K	HOH416
K	HOH424
K	HOH451
K	HOH453
K	HOH464
K	HOH497

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO I 301

Chain	Residue
I	ARG16
I	NDP302
I	HOH412
I	HOH589

site_id	AD8
Number of Residues	34
Details	binding site for residue NDP I 302

Chain	Residue
I	SER15
I	ARG16
I	GLY17
I	ILE18
I	TYR37
I	ALA38
I	GLY39
I	SER40
I	THR58
I	ASP59
I	SER60
I	ASN82
I	ALA83
I	GLY84
I	ILE85
I	ILE105
I	ILE130
I	GLY131
I	SER132
I	TYR146
I	LYS150
I	PRO176
I	GLY177
I	PRO178
I	ILE179
I	THR181
I	ALA183
I	ASN184
I	EDO301
I	HOH412
I	HOH422
I	HOH424
I	HOH433
I	HOH518

site_id	AD9
Number of Residues	5
Details	binding site for residue PG4 F 301

Chain	Residue
F	HIS240
H	GLY89
H	ALA141
H	GLY142
H	MET143

site_id	AE1
Number of Residues	37
Details	binding site for residue NDP F 302

Chain	Residue
F	GLY13
F	SER15
F	ARG16
F	GLY17
F	ILE18
F	TYR37
F	ALA38
F	GLY39
F	SER40
F	THR58
F	ASP59
F	SER60
F	ASN82
F	ALA83
F	GLY84
F	ILE85
F	ARG101
F	ILE105
F	ILE130
F	GLY131
F	SER132
F	TYR146
F	LYS150
F	PRO176
F	GLY177
F	PRO178
F	ILE179
F	THR181
F	ALA183
F	ASN184
F	HOH410
F	HOH419
F	HOH437
F	HOH447
F	HOH485
F	HOH487
F	HOH494

site_id	AE2
Number of Residues	1
Details	binding site for residue EDO G 301

Chain	Residue
G	HIS240

site_id	AE3
Number of Residues	32
Details	binding site for residue NDP G 302

Chain	Residue
G	GLY13
G	SER15
G	ARG16
G	GLY17
G	ILE18
G	TYR37
G	ALA38
G	GLY39
G	SER40
G	THR58
G	ASP59
G	SER60
G	ASN82
G	ALA83
G	GLY84
G	ILE105
G	ILE130
G	GLY131
G	SER132
G	TYR146
G	LYS150
G	PRO176
G	GLY177
G	PRO178
G	ILE179
G	THR181
G	ALA183
G	ASN184
G	HOH406
G	HOH407
G	HOH414
G	HOH418

site_id	AE4
Number of Residues	35
Details	binding site for residue NDP L 301

Chain	Residue
L	SER15
L	ARG16
L	GLY17
L	ILE18
L	TYR37
L	ALA38
L	GLY39
L	SER40
L	THR58
L	ASP59
L	SER60
L	ASN82
L	ALA83
L	GLY84
L	ILE85
L	ARG101
L	ILE105
L	ILE130
L	GLY131
L	SER132
L	TYR146
L	LYS150
L	PRO176
L	GLY177
L	PRO178
L	ILE179
L	THR181
L	ALA183
L	ASN184
L	HOH409
L	HOH439
L	HOH449
L	HOH504
L	HOH538
L	HOH540

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. VngdrmpvagMaaYAASKSALqGMArGLA

Chain	Residue	Details
A	VAL133-ALA161

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	300
Details	Binding site: {"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)