5MSR

Structure of the unmodified PCP-R domain of carboxylic acid reductase (CAR) from Segniliparus rugosus in complex with NADPH, P43 form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001676	biological_process	long-chain fatty acid metabolic process
A	0004467	molecular_function	long-chain fatty acid-CoA ligase activity
A	0005524	molecular_function	ATP binding
A	0006629	biological_process	lipid metabolic process
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0031177	molecular_function	phosphopantetheine binding
A	0050661	molecular_function	NADP binding
B	0000166	molecular_function	nucleotide binding
B	0001676	biological_process	long-chain fatty acid metabolic process
B	0004467	molecular_function	long-chain fatty acid-CoA ligase activity
B	0005524	molecular_function	ATP binding
B	0006629	biological_process	lipid metabolic process
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0031177	molecular_function	phosphopantetheine binding
B	0050661	molecular_function	NADP binding
C	0000166	molecular_function	nucleotide binding
C	0001676	biological_process	long-chain fatty acid metabolic process
C	0004467	molecular_function	long-chain fatty acid-CoA ligase activity
C	0005524	molecular_function	ATP binding
C	0006629	biological_process	lipid metabolic process
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0031177	molecular_function	phosphopantetheine binding
C	0050661	molecular_function	NADP binding
D	0000166	molecular_function	nucleotide binding
D	0001676	biological_process	long-chain fatty acid metabolic process
D	0004467	molecular_function	long-chain fatty acid-CoA ligase activity
D	0005524	molecular_function	ATP binding
D	0006629	biological_process	lipid metabolic process
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0031177	molecular_function	phosphopantetheine binding
D	0050661	molecular_function	NADP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue NAP A 1201

Chain	Residue
A	GLY799
A	SER894
A	GLY895
A	ALA896
A	VAL898
A	LEU933
A	SER934
A	TYR970
A	LYS974
A	SER997
A	HOH1302
A	ASN801
A	GLY802
A	TRP803
A	LEU804
A	ARG828
A	ARG838
A	ASP868
A	PHE869

---

site_id	AC2
Number of Residues	22
Details	binding site for residue NAP B 1201

Chain	Residue
B	GLY799
B	ASN801
B	GLY802
B	TRP803
B	LEU804
B	ARG828
B	ARG838
B	ASP868
B	PHE869
B	SER894
B	GLY895
B	ALA896
B	VAL898
B	LEU933
B	SER934
B	TYR970
B	LYS974
B	SER997
B	HOH1343
B	HOH1352
B	HOH1359
B	HOH1361

---

site_id	AC3
Number of Residues	22
Details	binding site for residue NAP C 1201

Chain	Residue
C	GLY799
C	ASN801
C	GLY802
C	TRP803
C	LEU804
C	ARG828
C	ARG838
C	ASP868
C	PHE869
C	SER894
C	GLY895
C	ALA896
C	VAL898
C	LEU933
C	SER934
C	TYR970
C	LYS974
C	SER997
C	HOH1303
C	HOH1326
C	HOH1331
C	HOH1334

---

site_id	AC4
Number of Residues	23
Details	binding site for residue NAP D 1201

Chain	Residue
D	GLY799
D	ASN801
D	GLY802
D	TRP803
D	LEU804
D	ARG828
D	ARG838
D	ASP868
D	PHE869
D	SER894
D	GLY895
D	ALA896
D	VAL898
D	LEU933
D	SER934
D	TYR970
D	LYS974
D	SER997
D	HOH1308
D	HOH1311
D	HOH1315
D	HOH1323
D	HOH1331

---

Functional Information from PROSITE/UniProt

site_id	PS00455
Number of Residues	12
Details	AMP_BINDING Putative AMP-binding domain signature. LIYTSGSTGtPK

Chain	Residue	Details
A	LEU262-LYS273

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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