3LVF

Crystal Structure of holo Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH1) from methicillin resistant Staphylococcus aureus MRSA252 at 1.7 Angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0000166	molecular_function	nucleotide binding
O	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O	0005737	cellular_component	cytoplasm
O	0006006	biological_process	glucose metabolic process
O	0006096	biological_process	glycolytic process
O	0016491	molecular_function	oxidoreductase activity
O	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O	0050661	molecular_function	NADP binding
O	0051287	molecular_function	NAD binding
P	0000166	molecular_function	nucleotide binding
P	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P	0005737	cellular_component	cytoplasm
P	0006006	biological_process	glucose metabolic process
P	0006096	biological_process	glycolytic process
P	0016491	molecular_function	oxidoreductase activity
P	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P	0050661	molecular_function	NADP binding
P	0051287	molecular_function	NAD binding
Q	0000166	molecular_function	nucleotide binding
Q	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q	0005737	cellular_component	cytoplasm
Q	0006006	biological_process	glucose metabolic process
Q	0006096	biological_process	glycolytic process
Q	0016491	molecular_function	oxidoreductase activity
Q	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q	0050661	molecular_function	NADP binding
Q	0051287	molecular_function	NAD binding
R	0000166	molecular_function	nucleotide binding
R	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R	0005737	cellular_component	cytoplasm
R	0006006	biological_process	glucose metabolic process
R	0006096	biological_process	glycolytic process
R	0016491	molecular_function	oxidoreductase activity
R	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R	0050661	molecular_function	NADP binding
R	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD P 337

Chain	Residue
P	GLY9
P	CYS96
P	THR97
P	GLY98
P	PHE99
P	SER120
P	ALA121
P	ASN316
P	TYR320
P	HOH341
P	HOH344
P	GLY11
P	HOH351
P	HOH368
P	HOH372
P	HOH377
P	HOH407
P	HOH427
P	HOH429
P	HOH430
P	HOH510
P	HOH566
P	ARG12
P	HOH576
Q	PRO190
Q	HOH342
P	ILE13
P	ASN33
P	ASP34
P	LEU35
P	GLU77
P	PRO78

---

site_id	AC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD R 337

Chain	Residue
O	PRO190
O	HOH372
R	GLY9
R	GLY11
R	ARG12
R	ILE13
R	ASN33
R	ASP34
R	LEU35
R	PRO78
R	CYS96
R	THR97
R	GLY98
R	PHE99
R	SER120
R	ALA121
R	THR181
R	ASN316
R	TYR320
R	HOH340
R	HOH342
R	HOH354
R	HOH387
R	HOH423
R	HOH433
R	HOH446
R	HOH449
R	HOH451
R	HOH454
R	HOH591
R	HOH618
R	HOH658

---

site_id	AC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD O 337

Chain	Residue
O	GLY9
O	GLY11
O	ARG12
O	ILE13
O	ASN33
O	ASP34
O	PRO78
O	CYS96
O	THR97
O	GLY98
O	SER120
O	ALA121
O	ASN316
O	TYR320
O	HOH343
O	HOH344
O	HOH348
O	HOH350
O	HOH362
O	HOH366
O	HOH384
O	HOH386
O	HOH419
O	HOH421
O	HOH434
O	HOH437
O	HOH449
O	HOH503
R	PRO190
R	HOH338

---

site_id	AC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD Q 337

Chain	Residue
Q	ILE13
Q	ASN33
Q	ASP34
Q	LEU35
Q	GLU77
Q	PRO78
Q	CYS96
Q	THR97
Q	GLY98
Q	PHE99
Q	SER120
Q	ALA121
Q	ASN316
Q	TYR320
Q	HOH357
Q	HOH365
Q	HOH370
Q	HOH380
Q	HOH382
Q	HOH391
Q	HOH404
Q	HOH421
Q	HOH461
Q	HOH527
Q	HOH589
Q	HOH688
P	PRO190
P	HOH406
Q	GLY9
Q	GLY11
Q	ARG12

---

Functional Information from PROSITE/UniProt

site_id	PS00071
Number of Residues	8
Details	GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNsL

Chain	Residue	Details
P	ALA149-LEU156

---

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. MSVGDRQLVKVAAWY

Chain	Residue	Details
P	MET300-TYR314

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of Staphylococcal GAPDH1 in a hexagonal space group.","authors":["Roychowdhury A.","Mukherjee S.","Dutta D.","Das A.K."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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