1HDG

THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS 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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 O 338

Chain	Residue
O	THR179
O	ARG195
O	ARG231
O	NAD336
O	HOH347
O	HOH361

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 O 339

Chain	Residue
O	HIS176
O	THR208
O	GLY209
O	HOH361
O	HOH362
O	HOH363
O	HOH364
O	SER148
O	CYS149
O	THR150

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 Q 338

Chain	Residue
Q	THR179
Q	ASP181
Q	ARG195
Q	ARG231
Q	NAD336
Q	HOH346
Q	HOH353
Q	HOH430

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 Q 339

Chain	Residue
Q	SER148
Q	CYS149
Q	THR150
Q	HIS176
Q	THR208
Q	GLY209
Q	HOH350
Q	HOH353
Q	HOH354
Q	HOH430

---

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAD O 336

Chain	Residue
O	GLY7
O	GLY9
O	ARG10
O	ILE11
O	ASN31
O	ASP32
O	LEU33
O	PRO77
O	SER95
O	THR96
O	GLY97
O	THR119
O	ALA120
O	ASN180
O	ASN313
O	TYR317
O	SO4338
O	HOH345
O	HOH346
O	HOH347
O	HOH348
O	HOH351
O	HOH366
O	HOH369
O	HOH422
O	HOH423
O	HOH424
O	HOH426
Q	HOH411

---

site_id	AC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD Q 336

Chain	Residue
Q	GLY7
Q	GLY9
Q	ARG10
Q	ILE11
Q	ASN31
Q	ASP32
Q	LEU33
Q	PRO77
Q	SER95
Q	THR96
Q	GLY97
Q	PHE99
Q	THR119
Q	ALA120
Q	ASN180
Q	ASN313
Q	TYR317
Q	SO4338
Q	HOH341
Q	HOH342
Q	HOH343
Q	HOH345
Q	HOH346
Q	HOH347
Q	HOH348
Q	HOH350
Q	HOH351
Q	HOH363
Q	HOH366
Q	HOH367

---

Functional Information from PROSITE/UniProt

site_id	PS00430
Number of Residues	70
Details	TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. arvaingfgrigrlvyriiyerknpdievvaindltdtktlahllkydsvhkkfpgkveyte.....................................................NSLIVDGK

Chain	Residue	Details
O	ALA1-LYS69

---

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

Chain	Residue	Details
O	ALA147-ILE154

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7877172","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"Q6GIL8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
O	CYS149
O	HIS176

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
Q	CYS149
Q	HIS176

---