1XYM

the role of the divalent metal ion in sugar binding, ring opening, and isomerization by d-xylose isomerase: replacement of a catalytic metal by an amino-acid

• Total interactions analyzed: 1
• Total true interactions: 1
• Strongest Interaction:
  • Chains: A-B
  • Int. Res.: 138
  • Norm. En. per Res.: -3.5014
• 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	-69.5553	-29.4315	-384.203	-483.1898	138	30	4	15410	10	66	70

Interface residues

• A-B: ALA142A, ALA147A, ALA223A, ALA261A, ALA28A, ALA528B, ALA642B, ALA647B, ALA723B, ALA761B, ARG139A, ARG187A, ARG22A, ARG258A, ARG291A, ARG30A, ARG522B, ARG530B, ARG639B, ARG687B, ARG758B, ARG791B, ASN184A, ASN591B, ASN606B, ASN684B, ASN91A, ASP100A, ASP189A, ASP23A, ASP254A, ASP256A, ASP27A, ASP286A, ASP294A, ASP523B, ASP527B, ASP600B, ASP689B, ASP754B, ASP756B, ASP786B, ASP794B, GLN20A, GLN248A, GLN255A, GLN520B, GLN748B, GLN755B, GLU143A, GLU185A, GLU293A, GLU643B, GLU685B, GLU793B, GLY101A, GLY138A, GLY141A, GLY188A, GLY21A, GLY250A, GLY262A, GLY26A, GLY521B, GLY526B, GLY601B, GLY638B, GLY641B, GLY688B, GLY750B, GLY762B, HIS219A, HIS53A, HIS553B, HIS595B, HIS719B, HIS95A, ILE190A, ILE251A, ILE690B, ILE751B, LEU257A, LEU592B, LEU757B, LEU92A, LYS148A, LYS180A, LYS182A, LYS252A, LYS288A, LYS599B, LYS648B, LYS682B, LYS752B, LYS788B, LYS99A, MET222A, MET722B, PHE25A, PHE525B, PHE560B, PHE593B, PHE598B, PHE60A, PHE93A, PHE98A, PRO183A, PRO186A, PRO24A, PRO289A, PRO290A, PRO524B, PRO596B, PRO683B, PRO686B, PRO789B, PRO790B, PRO96A, SER144A, SER249A, SER644B, SER749B, THR292A, THR29A, THR529B, THR594B, THR792B, THR94A, TRP136A, TRP15A, TRP19A, TRP515B, TRP519B, TRP636B, TYR253A, TYR753B, VAL597B, VAL97A