Table 3 Alignment of ACE residues involved in direct interactions with Ac-SDKP compared to the C-domain ACE-AngII and N-domain ACE-RXP407 complexes.
From: Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme
Position | N-AcSDKP | Ang II31 | RXP407 inhibitor30 | |||
---|---|---|---|---|---|---|
N-domain ACE | Corresponding residues in C-ACE | Corresponding residues in N-ACE | C-domain ACE | N-domain ACE | Corresponding residues in C-ACE | |
S2 | D336 | D358 | ||||
S2 | Y369 | F391 | Y369 | F391 | ||
S2 | H388 | H410 | ||||
S1 | A334 | A356 | A334 | A356 | A334 | A356 |
S1 | E362 | E384 | E362 | E384 | E362 | E384 |
S1 | T496 | V518 | ||||
S1′ | H331 | H353 | H331 | H353 | H331 | H353 |
S1′ | A332 | A354 | A332 | A354 | A332 | A354 |
S1′ | T358 | V518 | ||||
S1′ | H491 | H513 | H491 | H513 | H491 | H513 |
S1′ | Y501 | Y523 | Y501 | Y523 | Y501 | Y523 |
S2′ | Q259 | Q281 | Q259 | Q281 | Q259 | Q281 |
S2′ | K489 | K511 | K489 | K511 | K489 | K511 |
S2′ | Y498 | Y520 | Y498 | Y520 | Y498 | Y520 |