1FWR

CRYSTAL STRUCTURE OF KDPG ALDOLASE DOUBLE MUTANT K133Q/T161K

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008675	molecular_function	2-dehydro-3-deoxy-phosphogluconate aldolase activity
A	0008700	molecular_function	(R,S)-4-hydroxy-2-oxoglutarate aldolase activity
A	0008948	molecular_function	oxaloacetate decarboxylase activity
A	0009255	biological_process	Entner-Doudoroff pathway through 6-phosphogluconate
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0016833	molecular_function	oxo-acid-lyase activity
A	0042802	molecular_function	identical protein binding
A	0106009	molecular_function	(4S)-4-hydroxy-2-oxoglutarate aldolase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008675	molecular_function	2-dehydro-3-deoxy-phosphogluconate aldolase activity
B	0008700	molecular_function	(R,S)-4-hydroxy-2-oxoglutarate aldolase activity
B	0008948	molecular_function	oxaloacetate decarboxylase activity
B	0009255	biological_process	Entner-Doudoroff pathway through 6-phosphogluconate
B	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0016833	molecular_function	oxo-acid-lyase activity
B	0042802	molecular_function	identical protein binding
B	0106009	molecular_function	(4S)-4-hydroxy-2-oxoglutarate aldolase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008675	molecular_function	2-dehydro-3-deoxy-phosphogluconate aldolase activity
C	0008700	molecular_function	(R,S)-4-hydroxy-2-oxoglutarate aldolase activity
C	0008948	molecular_function	oxaloacetate decarboxylase activity
C	0009255	biological_process	Entner-Doudoroff pathway through 6-phosphogluconate
C	0016020	cellular_component	membrane
C	0016829	molecular_function	lyase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0016833	molecular_function	oxo-acid-lyase activity
C	0042802	molecular_function	identical protein binding
C	0106009	molecular_function	(4S)-4-hydroxy-2-oxoglutarate aldolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT A 214

Chain	Residue
A	GLU45
A	THR47
A	ARG49
A	THR73
A	SER93
A	PRO94
A	PHE135
C	PRO152

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIT B 214

Chain	Residue
B	GLU45
B	THR47
B	ARG49
B	THR73
B	SER93
B	PRO94
B	GLN133
B	PHE135
B	LYS161
A	PRO152

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT C 214

Chain	Residue
B	PRO152
C	VAL20
C	GLU45
C	ARG49
C	THR73
C	PRO94
C	GLN133
C	PHE135

---

Functional Information from PROSITE/UniProt

site_id	PS00159
Number of Residues	10
Details	ALDOLASE_KDPG_KHG_1 KDPG and KHG aldolases active site. GVrvlEVTLR

Chain	Residue	Details
A	GLY40-ARG49

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11342129","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16403639","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1978721","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11342129","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16403639","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"3136164","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EUA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EUA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Site: {"description":"Plays a major role in determining the stereoselectivity","evidences":[{"source":"PubMed","id":"17981470","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1fq0

Chain	Residue	Details
A	GLN133
A	GLU45

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1fq0

Chain	Residue	Details
B	GLN133
B	GLU45

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1fq0

Chain	Residue	Details
C	GLN133
C	GLU45

---

site_id	MCSA1
Number of Residues	3
Details	M-CSA 550

Chain	Residue	Details
A	GLU45	proton acceptor, proton donor
A	ARG49	electrostatic stabiliser, modifies pKa
A	GLN133	electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 550

Chain	Residue	Details
B	GLU45	proton acceptor, proton donor
B	ARG49	electrostatic stabiliser, modifies pKa
B	GLN133	electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 550

Chain	Residue	Details
C	GLU45	proton acceptor, proton donor
C	ARG49	electrostatic stabiliser, modifies pKa
C	GLN133	electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

---