2ATS

Dihydrodipicolinate synthase co-crystallised with (S)-lysine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
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	0019752	biological_process	carboxylic acid metabolic process
A	0019877	biological_process	diaminopimelate biosynthetic process
A	0042802	molecular_function	identical protein binding
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
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	0019752	biological_process	carboxylic acid metabolic process
B	0019877	biological_process	diaminopimelate biosynthetic process
B	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 1001

Chain	Residue
A	ALA152
A	VAL154
A	LYS155
A	ILE157
A	HOH3177
A	HOH3276

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 1002

Chain	Residue
B	ILE157
B	HOH2162
B	HOH2295
B	ALA152
B	VAL154
B	LYS155

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 2001

Chain	Residue
A	THR44
A	LEU101
A	LYS161
A	HOH3027

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 2002

Chain	Residue
B	THR44
B	LEU101
B	LYS161
B	HOH2025
B	HOH2034

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DLY A 3001

Chain	Residue
A	SER48
A	ALA49
A	LEU51
A	HIS53
A	HIS56
A	TYR106
A	DLY3002
A	HOH3046
A	HOH3056
B	ASN80
B	GLU84

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DLY A 3002

Chain	Residue
A	ASN80
A	GLU84
A	DLY3001
A	HOH3063
A	HOH3101
B	SER48
B	ALA49
B	LEU51
B	HIS56
B	TYR106

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DLY A 3003

Chain	Residue
A	HOH3020
A	HOH3092
A	HOH3141
B	ALA33
B	HOH2126

---

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

---

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

Chain	Residue	Details
A	TYR133-ALA163

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Schiff-base intermediate with substrate"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20353808","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22552955","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Part of a proton relay during catalysis"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"L-lysine inhibitor binding; via carbonyl oxygen"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Site: {"description":"L-lysine inhibitor binding"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
A	ARG138
A	TYR133
A	LYS161

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
B	ARG138
B	TYR133
B	LYS161

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
A	THR44
A	LYS161
A	THR45

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhp

Chain	Residue	Details
B	THR44
B	LYS161
B	THR45

---

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	ARG138	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

---

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	ARG138	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

---