1OZF

the crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 59
  • Norm. En. per Res.: -2.3889
• Hub Node: A(1)

All Interactions

Chains	Hydro. Bond Ener. (kJ/mol)	Elec. Ener. (kJ/mol)	VDW. Ener. (kJ/mol)	Tot. Stab. Ener. (kJ/mol)	#int. res.	# Short cont.	#Hydr. int.	#VDW pairs	#salt bridges	#Pot. fav. elec. int	#Pot. unfav. elec. int
A-B	-19.6232	-16.2191	-105.1	-140.9423	59	12	6	4926	1	27	24

Interface residues

• A-B: ALA112A, ALA112B, ALA115A, ALA115B, ALA126A, ALA126B, ALA135B, ALA140A, ALA140B, ALA143A, ALA143B, ALA145B, ARG111A, ARG111B, ASN150A, ASN150B, ASP113A, ASP113B, ASP123A, ASP123B, ASP142A, ASP142B, ASP170A, ASP170B, GLN117A, GLN117B, GLU137A, GLU137B, GLU146A, GLU146B, HIS119A, ILE136A, ILE136B, LEU144A, LEU144B, LYS110A, LYS110B, LYS114A, LYS114B, LYS116A, LYS116B, PRO141A, PRO141B, THR139A, THR139B, TYR134A, TYR134B, VAL109A, VAL109B, VAL118A, VAL125A, VAL125B, VAL138A, VAL138B, VAL147A, VAL147B, VAL148B, VAL165B, VAL171B