5UM0

Crystal structure of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Neisseria gonorrhoeae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004619	molecular_function	phosphoglycerate mutase activity
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B	0004619	molecular_function	phosphoglycerate mutase activity
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
C	0004619	molecular_function	phosphoglycerate mutase activity
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0016853	molecular_function	isomerase activity
C	0016868	molecular_function	intramolecular phosphotransferase activity
C	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
D	0004619	molecular_function	phosphoglycerate mutase activity
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016853	molecular_function	isomerase activity
D	0016868	molecular_function	intramolecular phosphotransferase activity
D	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue TLA A 300

Chain	Residue
A	ARG7
A	HOH403
A	HOH409
A	HOH423
A	HOH442
A	HOH447
A	HOH459
A	HOH528
A	HOH554
A	ASN14
A	LEU18
A	PHE19
A	THR20
A	GLY21
A	GLU86
A	TYR89
A	LYS97

---

site_id	AC2
Number of Residues	11
Details	binding site for residue TLA B 300

Chain	Residue
B	ARG7
B	PHE19
B	THR20
B	GLY21
B	GLU86
B	LYS97
B	ASN183
B	HOH454
B	HOH457
B	HOH473
B	HOH529

---

site_id	AC3
Number of Residues	16
Details	binding site for residue TLA C 300

Chain	Residue
C	ARG7
C	ASN14
C	LEU18
C	PHE19
C	THR20
C	GLY21
C	GLU86
C	TYR89
C	LYS97
C	ASN183
C	HOH403
C	HOH424
C	HOH447
C	HOH450
C	HOH504
C	HOH518

---

site_id	AC4
Number of Residues	11
Details	binding site for residue TLA D 300

Chain	Residue
D	ARG7
D	PHE19
D	THR20
D	GLY21
D	GLU86
D	TYR89
D	LYS97
D	ARG113
D	HOH411
D	HOH416
D	HOH418

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	HIS8
B	HIS8
C	HIS8
D	HIS8

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	GLU86
B	GLU86
C	GLU86
D	GLU86

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
B	THR20
B	ARG59
B	GLU86
B	LYS97
B	ARG113
B	GLY182
C	ARG7
C	THR20
C	ARG59
C	GLU86
C	LYS97
C	ARG113
C	GLY182
D	ARG7
D	THR20
D	ARG59
D	GLU86
D	LYS97
D	ARG113
D	GLY182
A	ARG113
A	ARG7
A	THR20
A	ARG59
A	GLU86
A	LYS97
A	GLY182
B	ARG7

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	HIS181
B	HIS181
C	HIS181
D	HIS181

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