Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NNE

Crystal structure of choline oxidase S101A mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0016491	molecular_function	oxidoreductase activity
A	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
A	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000166	molecular_function	nucleotide binding
B	0016491	molecular_function	oxidoreductase activity
B	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
B	0019285	biological_process	glycine betaine biosynthetic process from choline
B	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000166	molecular_function	nucleotide binding
C	0016491	molecular_function	oxidoreductase activity
C	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
C	0019285	biological_process	glycine betaine biosynthetic process from choline
C	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000166	molecular_function	nucleotide binding
D	0016491	molecular_function	oxidoreductase activity
D	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
D	0019285	biological_process	glycine betaine biosynthetic process from choline
D	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0000166	molecular_function	nucleotide binding
E	0016491	molecular_function	oxidoreductase activity
E	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
E	0019285	biological_process	glycine betaine biosynthetic process from choline
E	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0000166	molecular_function	nucleotide binding
F	0016491	molecular_function	oxidoreductase activity
F	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
F	0019285	biological_process	glycine betaine biosynthetic process from choline
F	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
F	0050660	molecular_function	flavin adenine dinucleotide binding
G	0000166	molecular_function	nucleotide binding
G	0016491	molecular_function	oxidoreductase activity
G	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
G	0019285	biological_process	glycine betaine biosynthetic process from choline
G	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
G	0050660	molecular_function	flavin adenine dinucleotide binding
H	0000166	molecular_function	nucleotide binding
H	0016491	molecular_function	oxidoreductase activity
H	0016614	molecular_function	oxidoreductase activity, acting on CH-OH group of donors
H	0019285	biological_process	glycine betaine biosynthetic process from choline
H	0033713	molecular_function	choline:oxygen 1-oxidoreductase activity
H	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD A 547

Chain	Residue
A	GLY20
A	ALA90
A	LYS91
A	VAL92
A	GLY95
A	CYS96
A	SER97
A	HIS99
A	ASN100
A	ALA101
A	CYS102
A	GLY22
A	ILE103
A	ALA232
A	SER268
A	THR269
A	GLY270
A	ASP273
A	TYR465
A	ASP499
A	ALA500
A	ASN510
A	SER23
A	PRO511
A	ASN512
A	VAL515
A	ACT601
A	ALA24
A	GLU44
A	ALA45
A	LEU65
A	TRP71
A	ARG89

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 601

Chain	Residue
A	VAL464
A	HIS466
A	ASN510
A	FAD547
A	HOH611

site_id	AC3
Number of Residues	35
Details	BINDING SITE FOR RESIDUE FAD B 547

Chain	Residue
B	GLY20
B	GLY22
B	SER23
B	ALA24
B	GLU44
B	ALA45
B	TRP71
B	ALA88
B	ARG89
B	ALA90
B	LYS91
B	VAL92
B	GLY95
B	CYS96
B	HIS99
B	ASN100
B	ALA101
B	CYS102
B	ILE103
B	LEU230
B	ARG231
B	ALA232
B	SER268
B	THR269
B	GLY270
B	ASP273
B	TYR465
B	ASP499
B	ALA500
B	ASN510
B	PRO511
B	ASN512
B	VAL515
B	ACT601
B	HOH616

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 601

Chain	Residue
B	ILE103
B	HIS351
B	VAL464
B	FAD547
B	HOH611

site_id	AC5
Number of Residues	34
Details	BINDING SITE FOR RESIDUE FAD C 547

Chain	Residue
C	ALA232
C	SER268
C	THR269
C	GLY270
C	ASP273
C	TYR465
C	ASP499
C	ALA500
C	ASN510
C	PRO511
C	ASN512
C	ACT601
C	HOH611
C	GLY20
C	GLY22
C	SER23
C	ALA24
C	GLU44
C	ALA45
C	TRP61
C	TRP71
C	ARG89
C	ALA90
C	LYS91
C	VAL92
C	GLY95
C	CYS96
C	HIS99
C	ASN100
C	ALA101
C	CYS102
C	ILE103
C	LEU230
C	ARG231

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT C 601

Chain	Residue
C	VAL464
C	FAD547
C	HOH611

site_id	AC7
Number of Residues	35
Details	BINDING SITE FOR RESIDUE FAD D 547

Chain	Residue
D	GLY20
D	GLY22
D	SER23
D	ALA24
D	GLU44
D	ALA45
D	TRP61
D	TRP71
D	ARG89
D	ALA90
D	LYS91
D	VAL92
D	GLY95
D	CYS96
D	HIS99
D	ASN100
D	ALA101
D	CYS102
D	ILE103
D	LEU230
D	ALA232
D	SER268
D	THR269
D	ASP273
D	TYR465
D	HIS466
D	ASP499
D	ALA500
D	ASN510
D	PRO511
D	ASN512
D	VAL515
D	ACT601
D	HOH613
D	HOH614

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT D 601

Chain	Residue
D	ILE103
D	HIS351
D	VAL464
D	FAD547
D	HOH611

site_id	AC9
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD E 547

Chain	Residue
E	GLY20
E	GLY22
E	SER23
E	ALA24
E	GLU44
E	ALA45
E	TRP71
E	ARG89
E	ALA90
E	LYS91
E	VAL92
E	GLY95
E	CYS96
E	HIS99
E	ASN100
E	ALA101
E	CYS102
E	ILE103
E	ARG231
E	ALA232
E	SER268
E	THR269
E	GLY270
E	ASP273
E	TYR465
E	HIS466
E	ASP499
E	ALA500
E	ASN510
E	PRO511
E	ASN512

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT E 601

Chain	Residue
E	TRP61
E	HOH611

site_id	BC2
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD F 547

Chain	Residue
F	GLY20
F	GLY22
F	SER23
F	ALA24
F	GLU44
F	ALA45
F	TRP71
F	ALA88
F	ARG89
F	ALA90
F	LYS91
F	VAL92
F	GLY95
F	CYS96
F	SER97
F	HIS99
F	ASN100
F	ALA101
F	CYS102
F	ILE103
F	LEU230
F	ALA232
F	SER268
F	THR269
F	GLY270
F	ASP273
F	TYR465
F	HIS466
F	ASP499
F	ALA500
F	ASN510
F	PRO511
F	ASN512
F	VAL515
F	ACT601
F	HOH629
F	HOH634

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT F 601

Chain	Residue
F	ILE103
F	HIS351
F	VAL464
F	FAD547
F	HOH611

site_id	BC4
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD G 547

Chain	Residue
G	GLY20
G	GLY22
G	SER23
G	ALA24
G	GLU44
G	ALA45
G	TRP71
G	ALA90
G	LYS91
G	VAL92
G	GLY95
G	CYS96
G	SER97
G	HIS99
G	ASN100
G	ALA101
G	CYS102
G	ILE103
G	LEU230
G	ARG231
G	ALA232
G	SER268
G	THR269
G	GLY270
G	ASP273
G	TYR465
G	HIS466
G	ASP499
G	ALA500
G	ASN510
G	PRO511
G	ASN512
G	VAL515
G	ACT601
G	HOH625
G	HOH653
G	HOH654

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT G 601

Chain	Residue
G	ALA101
G	VAL464
G	ASN510
G	FAD547
G	HOH611

site_id	BC6
Number of Residues	36
Details	BINDING SITE FOR RESIDUE FAD H 547

Chain	Residue
H	VAL19
H	GLY20
H	GLY22
H	SER23
H	ALA24
H	GLU44
H	ALA45
H	LEU65
H	TRP71
H	ARG89
H	ALA90
H	LYS91
H	VAL92
H	GLY95
H	CYS96
H	HIS99
H	ASN100
H	ALA101
H	CYS102
H	ILE103
H	ARG231
H	ALA232
H	SER268
H	THR269
H	ASP273
H	TYR465
H	HIS466
H	ASP499
H	ALA500
H	ASN510
H	PRO511
H	ASN512
H	VAL515
H	ACT601
H	HOH614
H	HOH629

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT H 601

Chain	Residue
H	VAL464
H	HIS466
H	ASN510
H	FAD547

Functional Information from PROSITE/UniProt

site_id	PS00624
Number of Residues	15
Details	GMC_OXRED_2 GMC oxidoreductases signature 2. GAidTPkLLmlSGIG

Chain	Residue	Details
A	GLY270-GLY284

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000250\|UniProtKB:E4QP00

Chain	Residue	Details
A	HIS466
B	HIS466
C	HIS466
D	HIS466
E	HIS466
F	HIS466
G	HIS466
H	HIS466

site_id	SWS_FT_FI2
Number of Residues	72
Details	BINDING:

Chain	Residue	Details
A	SER23
B	SER23
B	GLU44
B	TRP71
B	ALA90
B	CYS96
B	ALA232
B	TYR465
B	ALA500
B	ASN510
C	SER23
A	GLU44
C	GLU44
C	TRP71
C	ALA90
C	CYS96
C	ALA232
C	TYR465
C	ALA500
C	ASN510
D	SER23
D	GLU44
A	TRP71
D	TRP71
D	ALA90
D	CYS96
D	ALA232
D	TYR465
D	ALA500
D	ASN510
E	SER23
E	GLU44
E	TRP71
A	ALA90
E	ALA90
E	CYS96
E	ALA232
E	TYR465
E	ALA500
E	ASN510
F	SER23
F	GLU44
F	TRP71
F	ALA90
A	CYS96
F	CYS96
F	ALA232
F	TYR465
F	ALA500
F	ASN510
G	SER23
G	GLU44
G	TRP71
G	ALA90
G	CYS96
A	ALA232
G	ALA232
G	TYR465
G	ALA500
G	ASN510
H	SER23
H	GLU44
H	TRP71
H	ALA90
H	CYS96
H	ALA232
A	TYR465
H	TYR465
H	ALA500
H	ASN510
A	ALA500
A	ASN510

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Tele-8alpha-FAD histidine

Chain	Residue	Details
A	HIS99
B	HIS99
C	HIS99
D	HIS99
E	HIS99
F	HIS99
G	HIS99
H	HIS99

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