2A6L

Dihydrodipicolinate synthase (E. coli)- mutant R138H

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008840	molecular_function	4-hydroxy-tetrahydrodipicolinate synthase activity
A	0009085	biological_process	lysine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0016829	molecular_function	lyase activity
A	0019877	biological_process	diaminopimelate biosynthetic process
A	0042802	molecular_function	identical protein binding
A	0044281	biological_process	small molecule metabolic process
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008840	molecular_function	4-hydroxy-tetrahydrodipicolinate synthase activity
B	0009085	biological_process	lysine biosynthetic process
B	0009089	biological_process	lysine biosynthetic process via diaminopimelate
B	0016829	molecular_function	lyase activity
B	0019877	biological_process	diaminopimelate biosynthetic process
B	0042802	molecular_function	identical protein binding
B	0044281	biological_process	small molecule metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 600

Chain	Residue
A	ALA152
A	VAL154
A	LYS155
A	ILE157
A	HOH811

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 601

Chain	Residue
B	HOH708
B	ALA152
B	VAL154
B	LYS155
B	ILE157

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Functional Information from PROSITE/UniProt

site_id	PS00665
Number of Residues	18
Details	DHDPS_1 Dihydrodipicolinate synthase signature 1. AIVsvGTTGESatlnhdE

Chain	Residue	Details
A	ALA38-GLU55

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site_id	PS00666
Number of Residues	31
Details	DHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPshTgcdLlpetvgrlakvkn.IiGIKEA

Chain	Residue	Details
A	TYR133-ALA163

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor

Chain	Residue	Details
A	TYR133
B	TYR133

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Schiff-base intermediate with substrate

Chain	Residue	Details
A	LYS161
B	LYS161

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:20353808, ECO:0000269|PubMed:22552955

Chain	Residue	Details
A	THR45
B	THR45
B	ILE203
A	ILE203

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Part of a proton relay during catalysis

Chain	Residue	Details
B	THR44
B	TYR107
A	THR44
A	TYR107

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site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: L-lysine inhibitor binding; via carbonyl oxygen

Chain	Residue	Details
A	ALA49
B	ALA49

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site_id	SWS_FT_FI6
Number of Residues	6
Details	SITE: L-lysine inhibitor binding

Chain	Residue	Details
A	TYR106
B	ASN80
B	GLU84
B	TYR106
A	ASN80
A	GLU84

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 267

Chain	Residue	Details
A	THR44	hydrogen bond acceptor, hydrogen bond donor
A	TYR107	hydrogen bond donor
A	TYR133	activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	HIS138	electrostatic stabiliser
A	LYS161	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	ILE203	activator, increase electrophilicity, polar interaction, steric role

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 267

Chain	Residue	Details
B	THR44	hydrogen bond acceptor, hydrogen bond donor
B	TYR107	hydrogen bond donor
B	TYR133	activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	HIS138	electrostatic stabiliser
B	LYS161	covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
B	ILE203	activator, increase electrophilicity, polar interaction, steric role

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