Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5H5X

Crystal structure of NADH bound carbonyl reductase from Streptomyces coelicolor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0008202	biological_process	steroid metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0008202	biological_process	steroid metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0008202	biological_process	steroid metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0008202	biological_process	steroid metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0008202	biological_process	steroid metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0008202	biological_process	steroid metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
G	0000166	molecular_function	nucleotide binding
G	0008202	biological_process	steroid metabolic process
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
H	0000166	molecular_function	nucleotide binding
H	0008202	biological_process	steroid metabolic process
H	0016491	molecular_function	oxidoreductase activity
H	0046872	molecular_function	metal ion binding
I	0000166	molecular_function	nucleotide binding
I	0008202	biological_process	steroid metabolic process
I	0016491	molecular_function	oxidoreductase activity
I	0046872	molecular_function	metal ion binding
J	0000166	molecular_function	nucleotide binding
J	0008202	biological_process	steroid metabolic process
J	0016491	molecular_function	oxidoreductase activity
J	0046872	molecular_function	metal ion binding
K	0000166	molecular_function	nucleotide binding
K	0008202	biological_process	steroid metabolic process
K	0016491	molecular_function	oxidoreductase activity
K	0046872	molecular_function	metal ion binding
L	0000166	molecular_function	nucleotide binding
L	0008202	biological_process	steroid metabolic process
L	0016491	molecular_function	oxidoreductase activity
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue NAI A 301

Chain	Residue
A	GLY26
A	ASN103
A	ALA104
A	GLY105
A	VAL155
A	ALA156
A	TYR170
A	LYS174
A	PRO200
A	GLY201
A	ILE203
A	SER29
A	THR205
A	IPA302
A	HOH418
A	HOH444
A	HOH450
A	GLY30
A	ILE31
A	ASP50
A	PHE51
A	LEU75
A	ASP76
A	VAL77

site_id	AC2
Number of Residues	5
Details	binding site for residue IPA A 302

Chain	Residue
A	SER157
A	TYR170
A	PHE202
A	NAI301
A	IPA303

site_id	AC3
Number of Residues	3
Details	binding site for residue IPA A 303

Chain	Residue
A	SER167
A	TYR170
A	IPA302

site_id	AC4
Number of Residues	26
Details	binding site for residue NAI B 301

Chain	Residue
B	GLY26
B	ALA28
B	SER29
B	GLY30
B	ILE31
B	ASP50
B	PHE51
B	LEU75
B	ASP76
B	VAL77
B	ASN103
B	ALA104
B	GLY105
B	THR127
B	VAL155
B	ALA156
B	SER157
B	TYR170
B	LYS174
B	PRO200
B	GLY201
B	PHE202
B	ILE203
B	IPA302
B	HOH448
B	HOH454

site_id	AC5
Number of Residues	5
Details	binding site for residue IPA B 302

Chain	Residue
B	SER157
B	TYR170
B	PHE202
B	NAI301
B	IPA303

site_id	AC6
Number of Residues	4
Details	binding site for residue IPA B 303

Chain	Residue
B	GLY107
B	SER167
B	TYR170
B	IPA302

site_id	AC7
Number of Residues	23
Details	binding site for residue NAI C 301

Chain	Residue
C	GLY26
C	SER29
C	GLY30
C	ILE31
C	ASP50
C	PHE51
C	LEU75
C	ASP76
C	VAL77
C	ASN103
C	VAL155
C	ALA156
C	TYR170
C	LYS174
C	PRO200
C	GLY201
C	ILE203
C	THR205
C	IPA302
C	HOH404
C	HOH414
C	HOH416
C	HOH420

site_id	AC8
Number of Residues	4
Details	binding site for residue IPA C 302

Chain	Residue
C	SER157
C	TYR170
C	PHE202
C	NAI301

site_id	AC9
Number of Residues	6
Details	binding site for residue MG C 303

Chain	Residue
C	HOH442
A	VAL263
A	HOH415
A	HOH423
A	HOH476
C	VAL263

site_id	AD1
Number of Residues	2
Details	binding site for residue IPA C 304

Chain	Residue
C	SER167
C	TYR170

site_id	AD2
Number of Residues	27
Details	binding site for residue NAI D 301

Chain	Residue
D	GLY26
D	SER29
D	GLY30
D	ILE31
D	ASP50
D	PHE51
D	LEU75
D	ASP76
D	VAL77
D	ASN103
D	ALA104
D	GLY105
D	THR127
D	VAL155
D	ALA156
D	TYR170
D	LYS174
D	PRO200
D	GLY201
D	ILE203
D	THR205
D	IPA302
D	HOH404
D	HOH405
D	HOH433
D	HOH440
D	HOH452

site_id	AD3
Number of Residues	4
Details	binding site for residue IPA D 302

Chain	Residue
D	SER157
D	TYR170
D	PHE202
D	NAI301

site_id	AD4
Number of Residues	6
Details	binding site for residue MG D 303

Chain	Residue
B	VAL263
B	HOH409
B	HOH413
B	HOH423
B	HOH475
D	VAL263

site_id	AD5
Number of Residues	29
Details	binding site for residue NAI E 301

Chain	Residue
E	GLY26
E	SER29
E	GLY30
E	ILE31
E	ASP50
E	PHE51
E	LEU75
E	ASP76
E	VAL77
E	ASN103
E	ALA104
E	GLY105
E	THR127
E	VAL155
E	ALA156
E	SER157
E	TYR170
E	LYS174
E	PRO200
E	GLY201
E	PHE202
E	ILE203
E	THR205
E	PRO206
E	IPA303
E	HOH405
E	HOH440
E	HOH450
E	HOH453

site_id	AD6
Number of Residues	6
Details	binding site for residue MG E 302

Chain	Residue
E	VAL263
G	VAL263
G	HOH424
G	HOH432
G	HOH433
G	HOH460

site_id	AD7
Number of Residues	5
Details	binding site for residue IPA E 303

Chain	Residue
E	SER157
E	TYR170
E	PHE202
E	NAI301
E	IPA304

site_id	AD8
Number of Residues	3
Details	binding site for residue IPA E 304

Chain	Residue
E	SER167
E	TYR170
E	IPA303

site_id	AD9
Number of Residues	24
Details	binding site for residue NAI F 301

Chain	Residue
F	GLY26
F	SER29
F	GLY30
F	ILE31
F	ASP50
F	PHE51
F	LEU75
F	ASP76
F	VAL77
F	ASN103
F	ALA104
F	GLY105
F	VAL155
F	ALA156
F	TYR170
F	LYS174
F	PRO200
F	GLY201
F	ILE203
F	THR205
F	IPA302
F	HOH414
F	HOH420
F	HOH423

site_id	AE1
Number of Residues	4
Details	binding site for residue IPA F 302

Chain	Residue
F	SER157
F	TYR170
F	PHE202
F	NAI301

site_id	AE2
Number of Residues	3
Details	binding site for residue IPA F 303

Chain	Residue
F	SER167
F	TYR170
F	HOH456

site_id	AE3
Number of Residues	21
Details	binding site for residue NAI G 301

Chain	Residue
G	GLY26
G	SER29
G	GLY30
G	ILE31
G	ASP50
G	PHE51
G	LEU75
G	ASP76
G	VAL77
G	ASN103
G	ALA104
G	GLY105
G	VAL155
G	ALA156
G	TYR170
G	LYS174
G	PRO200
G	GLY201
G	ILE203
G	IPA302
G	HOH448

site_id	AE4
Number of Residues	6
Details	binding site for residue IPA G 302

Chain	Residue
G	SER157
G	LEU159
G	TYR170
G	PHE202
G	NAI301
G	IPA303

site_id	AE5
Number of Residues	3
Details	binding site for residue IPA G 303

Chain	Residue
G	GLY107
G	SER167
G	IPA302

site_id	AE6
Number of Residues	24
Details	binding site for residue NAI H 301

Chain	Residue
H	GLY26
H	SER29
H	GLY30
H	ILE31
H	ASP50
H	PHE51
H	LEU75
H	ASP76
H	VAL77
H	THR78
H	ASN103
H	ALA104
H	GLY105
H	VAL155
H	ALA156
H	TYR170
H	LYS174
H	PRO200
H	GLY201
H	ILE203
H	THR205
H	IPA303
H	HOH414
H	HOH440

site_id	AE7
Number of Residues	6
Details	binding site for residue MG H 302

Chain	Residue
F	VAL263
F	HOH418
H	VAL263
H	HOH421
H	HOH426
H	HOH451

site_id	AE8
Number of Residues	6
Details	binding site for residue IPA H 303

Chain	Residue
H	SER157
H	LEU159
H	TYR170
H	PHE202
H	NAI301
H	IPA304

site_id	AE9
Number of Residues	5
Details	binding site for residue IPA H 304

Chain	Residue
H	GLY107
H	GLY108
H	SER167
H	TYR170
H	IPA303

site_id	AF1
Number of Residues	24
Details	binding site for residue NAI I 301

Chain	Residue
I	GLY26
I	ALA28
I	SER29
I	GLY30
I	ILE31
I	ASP50
I	PHE51
I	LEU75
I	ASP76
I	VAL77
I	ASN103
I	ALA104
I	GLY105
I	VAL155
I	ALA156
I	SER157
I	TYR170
I	LYS174
I	PRO200
I	GLY201
I	ILE203
I	THR205
I	IPA304
I	HOH404

site_id	AF2
Number of Residues	5
Details	binding site for residue MG I 302

Chain	Residue
I	VAL263
I	HOH414
K	VAL263
K	HOH404
K	HOH456

site_id	AF3
Number of Residues	4
Details	binding site for residue IPA I 303

Chain	Residue
I	GLY107
I	SER167
I	TYR170
I	IPA304

site_id	AF4
Number of Residues	5
Details	binding site for residue IPA I 304

Chain	Residue
I	SER157
I	TYR170
I	PHE202
I	NAI301
I	IPA303

site_id	AF5
Number of Residues	21
Details	binding site for residue NAI J 301

Chain	Residue
J	GLY26
J	SER29
J	GLY30
J	ILE31
J	ASP50
J	PHE51
J	LEU75
J	ASP76
J	VAL77
J	ASN103
J	GLY105
J	VAL155
J	ALA156
J	SER157
J	TYR170
J	LYS174
J	PRO200
J	GLY201
J	ILE203
J	THR205
J	IPA302

site_id	AF6
Number of Residues	3
Details	binding site for residue IPA J 302

Chain	Residue
J	SER157
J	TYR170
J	NAI301

site_id	AF7
Number of Residues	24
Details	binding site for residue NAI K 301

Chain	Residue
K	GLY26
K	SER29
K	ILE31
K	ASP50
K	PHE51
K	LEU75
K	ASP76
K	VAL77
K	ASN103
K	ALA104
K	GLY105
K	THR127
K	VAL155
K	ALA156
K	SER157
K	TYR170
K	LYS174
K	PRO200
K	GLY201
K	ILE203
K	IPA303
K	HOH424
K	HOH436
K	HOH473

site_id	AF8
Number of Residues	3
Details	binding site for residue IPA K 302

Chain	Residue
K	SER167
K	TYR170
K	IPA303

site_id	AF9
Number of Residues	5
Details	binding site for residue IPA K 303

Chain	Residue
K	SER157
K	LEU159
K	TYR170
K	NAI301
K	IPA302

site_id	AG1
Number of Residues	22
Details	binding site for residue NAI L 301

Chain	Residue
L	GLY26
L	SER29
L	GLY30
L	ILE31
L	ASP50
L	PHE51
L	LEU75
L	ASP76
L	VAL77
L	ASN103
L	ALA104
L	GLY105
L	VAL155
L	ALA156
L	TYR170
L	LYS174
L	PRO200
L	GLY201
L	ILE203
L	IPA304
L	HOH414
L	HOH418

site_id	AG2
Number of Residues	6
Details	binding site for residue MG L 302

Chain	Residue
J	VAL263
J	HOH403
J	HOH420
J	HOH460
J	HOH468
L	VAL263

site_id	AG3
Number of Residues	5
Details	binding site for residue IPA L 303

Chain	Residue
L	GLY107
L	GLY108
L	SER167
L	TYR170
L	IPA304

site_id	AG4
Number of Residues	5
Details	binding site for residue IPA L 304

Chain	Residue
L	SER157
L	TYR170
L	PHE202
L	NAI301
L	IPA303

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER157-ALA185

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