1KOJ

Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004347	molecular_function	glucose-6-phosphate isomerase activity
A	0005125	molecular_function	cytokine activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0007165	biological_process	signal transduction
A	0016853	molecular_function	isomerase activity
A	0048029	molecular_function	monosaccharide binding
A	0051156	biological_process	glucose 6-phosphate metabolic process
A	0097367	molecular_function	carbohydrate derivative binding
A	1901135	biological_process	carbohydrate derivative metabolic process
B	0004347	molecular_function	glucose-6-phosphate isomerase activity
B	0005125	molecular_function	cytokine activity
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0007165	biological_process	signal transduction
B	0016853	molecular_function	isomerase activity
B	0048029	molecular_function	monosaccharide binding
B	0051156	biological_process	glucose 6-phosphate metabolic process
B	0097367	molecular_function	carbohydrate derivative binding
B	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PAN B 901

Chain	Residue
A	HIS388
B	GLY271
B	ARG272
B	GLN353
B	GLU357
B	LYS518
B	HOH948
B	HOH1015
B	HOH1094
B	HOH1130
B	HOH1159
B	ILE156
B	GLY157
B	GLY158
B	SER159
B	SER209
B	LYS210
B	THR211
B	THR214

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PAN A 902

Chain	Residue
A	ILE156
A	GLY157
A	GLY158
A	SER159
A	SER209
A	LYS210
A	THR211
A	THR214
A	GLY271
A	ARG272
A	GLN353
A	GLU357
A	LYS518
A	HOH1011
A	HOH1012
A	HOH1082
A	HOH1225
B	HIS388

---

Functional Information from PROSITE/UniProt

site_id	PS00174
Number of Residues	18
Details	P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GvVWdinsFDQwGVElgK

Chain	Residue	Details
A	GLY501-LYS518

---

site_id	PS00765
Number of Residues	14
Details	P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG

Chain	Residue	Details
A	ASP267-GLY280

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306

Chain	Residue	Details
A	SER358
B	SER358

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11327814, ECO:0000269|PubMed:11425306

Chain	Residue	Details
A	ALA389
A	GLN519
B	ALA389
B	GLN519

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:11425306, ECO:0007744|PDB:1HOX

Chain	Residue	Details
A	SER159
B	ALA389
A	LYS210
A	GLY354
A	SER358
A	ALA389
B	SER159
B	LYS210
B	GLY354
B	SER358

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	GLN519
B	GLN519

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	ALA2
B	ALA2

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	LEU12
A	GLY142
B	LEU12
B	GLY142

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	GLU34
B	GLU34

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	ASN107
A	PRO455
B	ASN107
B	PRO455

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	PRO109
B	PRO109

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744

Chain	Residue	Details
A	ASN185
B	ASN185

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0

Chain	Residue	Details
A	ALA250
B	ALA250

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	SER454
B	SER454

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	7
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	HIS388
B	ARG272
B	LYS518
B	GLU216
B	GLU357
B	LYS210
B	GLY271

---

site_id	CSA2
Number of Residues	7
Details	Annotated By Reference To The Literature 1dqr

Chain	Residue	Details
A	ARG272
A	LYS518
A	GLU216
A	GLU357
A	LYS210
A	GLY271
B	HIS388

---

site_id	MCSA1
Number of Residues	7
Details	M-CSA 842

Chain	Residue	Details
A	THR211	electrostatic stabiliser
A	THR217	modifies pKa
A	ARG272	electrostatic stabiliser
A	TYR273	electrostatic stabiliser
A	SER358	proton acceptor, proton donor
A	ALA389	proton acceptor, proton donor
A	GLN519	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 842

Chain	Residue	Details
B	THR211	electrostatic stabiliser
B	THR217	modifies pKa
B	ARG272	electrostatic stabiliser
B	TYR273	electrostatic stabiliser
B	SER358	proton acceptor, proton donor
B	ALA389	proton acceptor, proton donor
B	GLN519	proton acceptor, proton donor

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