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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	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	0071704	biological_process	obsolete organic substance metabolic 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	1
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:23517223

Chain	Residue	Details
A	ARG20

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Non-phosphorylated intermediate => ECO:0000305\|PubMed:11839312, ECO:0000305\|PubMed:14725765, ECO:0000305\|PubMed:16880541

Chain	Residue	Details
A	SER108

site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:23517223

Chain	Residue	Details
A	HIS329

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:14725765, ECO:0007744\|PDB:1PCJ

Chain	Residue	Details
A	TYR17
A	HIS308
A	GLU325
A	ARG421

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: via phosphate group => ECO:0000269\|PubMed:11839312, ECO:0000269\|PubMed:14725765, ECO:0000269\|PubMed:16595672, ECO:0000269\|PubMed:16880541, ECO:0000269\|PubMed:18690721, ECO:0000269\|PubMed:23517223

Chain	Residue	Details
A	SER108

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:11839312, ECO:0000269\|PubMed:14725765, ECO:0000269\|PubMed:16595672, ECO:0000269\|PubMed:16880541, ECO:0000269\|PubMed:18690721, ECO:0000269\|PubMed:22242625, ECO:0000269\|PubMed:23517223, ECO:0000269\|PubMed:24403075

Chain	Residue	Details
A	ASP242
A	ASP244
A	ASP246

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:14725765, ECO:0000269\|PubMed:18690721, ECO:0007744\|PDB:1P5D, ECO:0007744\|PDB:3BKQ

Chain	Residue	Details
A	LYS285

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:11839312, ECO:0000269\|PubMed:14725765, ECO:0000269\|PubMed:16595672, ECO:0000269\|PubMed:16880541

Chain	Residue	Details
A	SER108

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

221716

PDB entries from 2024-06-26

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