5KK0

Synechocystis ACO mutant - T136A

Replaces:  5E47

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0010436	molecular_function	carotenoid dioxygenase activity
A	0016121	biological_process	carotene catabolic process
A	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0102162	molecular_function	all-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
B	0010436	molecular_function	carotenoid dioxygenase activity
B	0016121	biological_process	carotene catabolic process
B	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
B	0102162	molecular_function	all-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
C	0010436	molecular_function	carotenoid dioxygenase activity
C	0016121	biological_process	carotene catabolic process
C	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0102162	molecular_function	all-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity
D	0010436	molecular_function	carotenoid dioxygenase activity
D	0016121	biological_process	carotene catabolic process
D	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
D	0102162	molecular_function	all-trans-8'-apo-beta-carotenal 15,15'-oxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue FE2 A 501

Chain	Residue
A	HIS183
A	HIS238
A	HIS304
A	HIS484
A	HOH611

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site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 502

Chain	Residue
A	ASN338
A	ASN341
C	ASP32

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site_id	AC3
Number of Residues	5
Details	binding site for residue FE2 B 501

Chain	Residue
B	HIS238
B	HIS304
B	HIS484
B	HOH613
B	HIS183

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site_id	AC4
Number of Residues	5
Details	binding site for residue FE2 C 501

Chain	Residue
C	HIS183
C	HIS238
C	HIS304
C	HIS484
C	HOH610

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site_id	AC5
Number of Residues	4
Details	binding site for residue CL D 501

Chain	Residue
B	ASN338
B	ASN341
D	TRP31
D	ASP32

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site_id	AC6
Number of Residues	4
Details	binding site for residue FE2 D 502

Chain	Residue
D	HIS183
D	HIS238
D	HIS304
D	HIS484

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:15821095

Chain	Residue	Details
A	HIS183
B	PHE303
B	HIS304
B	HIS484
C	HIS183
C	SER206
C	HIS238
C	PHE303
C	HIS304
C	HIS484
D	HIS183
A	SER206
D	SER206
D	HIS238
D	PHE303
D	HIS304
D	HIS484
A	HIS238
A	PHE303
A	HIS304
A	HIS484
B	HIS183
B	SER206
B	HIS238

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