2Q9J

Crystal structure of the C217S mutant of diaminopimelate epimerase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008837	molecular_function	diaminopimelate epimerase activity
A	0009085	biological_process	lysine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 440

Chain	Residue
A	TYR139
A	ILE140
A	ARG184
A	HOH562

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 441

Chain	Residue
A	CYS79
A	GLY8
A	PHE13
A	ASN75
A	GLY76
A	ARG78

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Functional Information from PROSITE/UniProt

site_id	PS01326
Number of Residues	15
Details	DAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevsqCGNGaR

Chain	Residue	Details
A	ASN64-ARG78

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ

Chain	Residue	Details
A	CSO73

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ

Chain	Residue	Details
A	SER217

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ

Chain	Residue	Details
A	ASN11
A	ASN64
A	ASN190
A	GLU208
A	GLY218
A	GLY74
A	ASN157

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKJ

Chain	Residue	Details
A	GLN44

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site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000305|PubMed:9843410, ECO:0007744|PDB:1BWZ

Chain	Residue	Details
A	GLU208
A	HIS159

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Important for dimerization => ECO:0000250|UniProtKB:P0A6K1

Chain	Residue	Details
A	TYR268

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 334

Chain	Residue	Details
A	CSO73	hydrogen bond acceptor, proton acceptor
A	HIS159	activator, electrostatic stabiliser
A	GLU208	activator, electrostatic stabiliser
A	SER217	hydrogen bond donor, proton donor
A	GLY220	electrostatic stabiliser, hydrogen bond donor

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