Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MRQ

Crystal Structure of wild-type unphosphorylated PMM/PGM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004614	molecular_function	phosphoglucomutase activity
A	0004615	molecular_function	phosphomannomutase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0009103	biological_process	lipopolysaccharide biosynthetic process
A	0009243	biological_process	O antigen biosynthetic process
A	0009244	biological_process	lipopolysaccharide core region biosynthetic process
A	0009298	biological_process	GDP-mannose biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0042121	biological_process	alginic acid biosynthetic process
A	0046872	molecular_function	metal ion binding
A	1901137	biological_process	carbohydrate derivative biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	LYS118
A	ASP242
A	ASP244
A	ASP246
A	TLA502

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TLA A 502

Chain	Residue
A	ASP242
A	ASP244
A	ASP246
A	ARG247
A	HIS329
A	ZN501
A	HOH745
A	ARG15
A	SER108
A	HIS109
A	LYS118

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	THR404
A	THR405
A	LEU406

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 504

Chain	Residue
A	GLU375
A	ARG432

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 505

Chain	Residue
A	GLU30
A	GLN67
A	PGE510

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG A 506

Chain	Residue
A	ILE138

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 507

Chain	Residue
A	TYR92
A	VAL96

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 508

Chain	Residue
A	ASN128
A	LYS305
A	LEU310
A	HOH684

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGE A 509

Chain	Residue
A	LEU266
A	LYS269
A	SER273
A	HOH655

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGE A 510

Chain	Residue
A	ASP74
A	GLY146
A	PEG505

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE A 511

Chain	Residue
A	ARG288
A	ALA292
A	ASP383
A	PRO414
A	HOH814
A	HOH817

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 512

Chain	Residue
A	PRO301
A	VAL302
A	MET303
A	HOH735
A	HOH781

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 513

Chain	Residue
A	ARG421
A	SER423
A	ASN424
A	THR425

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 514

Chain	Residue
A	ARG335
A	PHE337

Functional Information from PROSITE/UniProt

site_id	PS00710
Number of Residues	10
Details	PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmLTGSHNP

Chain	Residue	Details
A	GLY102-PRO111

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	129
Details	Region: {"description":"Topological domain 1","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	96
Details	Region: {"description":"Topological domain 2","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	104
Details	Region: {"description":"Topological domain 3","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	78
Details	Region: {"description":"Topological domain 4","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Active site: {"description":"Non-phosphorylated intermediate","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PCJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Binding site: {"description":"via phosphate group","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16595672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18690721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16595672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18690721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22242625","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24403075","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18690721","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P5D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BKQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16595672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 194

Chain	Residue	Details
A	ARG20	electrostatic stabiliser, hydrogen bond donor
A	SER108	metal ligand, nucleofuge, nucleophile
A	HIS109	electrostatic stabiliser, hydrogen bond donor
A	LYS118	electrostatic stabiliser, hydrogen bond donor
A	ASP242	metal ligand
A	ASP244	metal ligand
A	ASP246	metal ligand
A	ARG247	electrostatic stabiliser, hydrogen bond donor
A	HIS329	electrostatic stabiliser, polar interaction

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