Table 1: The zinc coordination residues and the residues that fix the coordination with hydrogen bonds.

Zinc metalloproteaseCoordination residuesResidues that form the hydrogen bond with the coordination residuesPDB no.

(1) Thermolysin type(HExxH- aan-E)α-helix-aan-α-helix
 ThermolysinHis142, His146 Glu166Asp170-2.8 Å-His142
Asn165-2.8 Å-His146
1KEI
 VibriolysinHis345, His349 Glu369Asp373-2.8 Å-His345
Asn368-2.8 Å-His349
3NQX
 Staphylococcus aureus  metalloproteinaseHis144, His148 Glu168Asn167-2.8 Å-His148
Asp172-2.8 Å-His144
1BQB
 Zinc aminopeptidaseHis265, His269 Glu288Phe272(C=O)-2.9 Å-His2691Z1W
 Leukotriene A4 hydrolaseHis295, His299 Glu318Glu325-2.8 Å-His295
Gly303(C=O)-2.6 Å-His299
1SQM
 Human thimet oligopeptidaseHis473, His477 Glu502Glu509-2.6 Å-His4731SQM
 Human neutral endopeptidase  (Neprilysin)His583, His587 Glu646Asp650-2.9 Å-His583
Asp590-2.7 Å-His587
1DMT

(2) Endopeptidase type(HExxH-aan-E or D) α-helix-aan-random coil
 Peptidyl-Lys metalloendopeptidaseHis117, His121 Asp130Asp154-2.7 Å-His117
Thr128(C=O)-2.8 Å-His121
1GE6

(3) Carboxypeptidase A typeβ-sheet-aan-random coil
 Carboxypeptidase AHis69, His196 Glu72Asp142-2.7 Å-His691YME
 Putative lysostaphin peptidaseHis232, His311 Asp236Glu315-2.6 Å-His311
Gly216(C=O)-2.8 Å-His232
2GU1