Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HJA

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Borrelia burgdorferi

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
A	0006096	biological_process	glycolytic process
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006006	biological_process	glucose metabolic process
B	0006096	biological_process	glycolytic process
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006006	biological_process	glucose metabolic process
C	0006096	biological_process	glycolytic process
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006006	biological_process	glucose metabolic process
D	0006096	biological_process	glycolytic process
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 336

Chain	Residue
A	SER152
A	CYS153
A	THR154
A	HIS180
A	THR211
A	ARG234
A	HOH408
A	HOH411

site_id	AC2
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD A 337

Chain	Residue
A	GLY9
A	ARG10
A	ILE11
A	ASN30
A	ASP31
A	LEU32
A	ARG75
A	SER93
A	THR94
A	GLY95
A	PHE97
A	THR122
A	VAL123
A	ASN184
A	ASN318
A	TYR322
A	SO4338
A	HOH342
A	HOH358
A	HOH385
A	HOH397
A	HOH439
A	HOH447
A	HOH573
A	HOH599
A	HOH757
A	HOH758
A	HOH759
B	LEU191
B	HOH354
A	GLY7

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

Chain	Residue
A	THR183
A	ASP185
A	ARG198
A	ARG234
A	NAD337
A	HOH358
A	HOH411
A	HOH776

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 339

Chain	Residue
A	LYS215
A	ASN229
A	HOH359
A	HOH446

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 336

Chain	Residue
B	SER152
B	CYS153
B	THR154
B	HIS180
B	THR211
B	ARG234
B	HOH372
B	HOH471
B	HOH769

site_id	AC6
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAD B 337

Chain	Residue
A	LEU191
A	HOH346
B	GLY7
B	GLY9
B	ARG10
B	ILE11
B	ASN30
B	ASP31
B	LEU32
B	ARG75
B	SER93
B	THR94
B	GLY95
B	PHE97
B	THR122
B	VAL123
B	ASN184
B	ASN318
B	TYR322
B	SO4338
B	HOH347
B	HOH352
B	HOH363
B	HOH368
B	HOH396
B	HOH423
B	HOH430
B	HOH466
B	HOH472
B	HOH614
B	HOH761
B	HOH762
B	HOH763
B	HOH764
B	HOH784

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 338

Chain	Residue
B	NAD337
B	HOH368
B	HOH471
B	HOH589
B	THR183
B	ASP185
B	ARG198
B	ARG234

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 339

Chain	Residue
B	LYS215
B	ASN229
B	HOH348

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 336

Chain	Residue
C	SER152
C	CYS153
C	THR154
C	THR211
C	ARG234
C	HOH419
C	HOH424

site_id	BC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD C 337

Chain	Residue
C	GLY7
C	GLY9
C	ARG10
C	ILE11
C	ASN30
C	ASP31
C	LEU32
C	ARG75
C	SER93
C	THR94
C	GLY95
C	PHE97
C	THR122
C	VAL123
C	ASN184
C	ASN318
C	TYR322
C	SO4338
C	HOH340
C	HOH351
C	HOH364
C	HOH365
C	HOH366
C	HOH372
C	HOH391
C	HOH400
C	HOH426
C	HOH721
C	HOH774
C	HOH855
D	LEU191
D	HOH359

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 338

Chain	Residue
C	THR183
C	ASP185
C	ARG198
C	ARG234
C	NAD337
C	HOH400
C	HOH857

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 339

Chain	Residue
B	MET303
C	LYS215
C	ASN229
C	HOH466

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 D 336

Chain	Residue
D	SER152
D	CYS153
D	THR154
D	HIS180
D	THR211
D	ARG234
D	HOH390
D	HOH419
D	HOH603

site_id	BC5
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAD D 337

Chain	Residue
C	LEU191
C	HOH352
D	GLY7
D	GLY9
D	ARG10
D	ILE11
D	ASN30
D	ASP31
D	LEU32
D	ARG75
D	SER93
D	THR94
D	GLY95
D	PHE97
D	THR122
D	VAL123
D	ASN184
D	ASN318
D	TYR322
D	SO4338
D	HOH347
D	HOH348
D	HOH350
D	HOH375
D	HOH384
D	HOH386
D	HOH387
D	HOH394
D	HOH427
D	HOH562
D	HOH753
D	HOH754
D	HOH755

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 338

Chain	Residue
D	THR183
D	ASP185
D	ARG198
D	ARG234
D	NAD337
D	HOH375
D	HOH848

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 339

Chain	Residue
A	MET303
D	LYS215
D	ASN229
D	HOH701
D	HOH750

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA151-LEU158

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAY-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Borrelia burgdorferi.","authoringGroup":["Seattle structural genomics center for infectious disease (SSGCID)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Borrelia burgdorferi.","authoringGroup":["Seattle structural genomics center for infectious disease (SSGCID)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"P00362","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
A	HIS180
A	CYS153

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

Chain	Residue	Details
B	HIS180
B	CYS153

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
C	HIS180
C	CYS153

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
D	HIS180
D	CYS153

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