Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047658 | molecular_function | alpha-amino-acid esterase activity |
| B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047658 | molecular_function | alpha-amino-acid esterase activity |
| C | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047658 | molecular_function | alpha-amino-acid esterase activity |
| D | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047658 | molecular_function | alpha-amino-acid esterase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 638 |
| Chain | Residue |
| A | GLU322 |
| A | ASP325 |
| A | ASN328 |
| A | ASN331 |
| A | HOH3051 |
| A | HOH3085 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 638 |
| Chain | Residue |
| B | ASN331 |
| B | HOH3021 |
| B | HOH3032 |
| B | GLU322 |
| B | ASP325 |
| B | ASN328 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 638 |
| Chain | Residue |
| C | GLU322 |
| C | ASP325 |
| C | ASN328 |
| C | ASN331 |
| C | HOH3019 |
| C | HOH3064 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 638 |
| Chain | Residue |
| D | GLU322 |
| D | ASP325 |
| D | ASN328 |
| D | ASN331 |
| D | HOH3052 |
| D | HOH3092 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 3001 |
| Chain | Residue |
| C | ARG55 |
| C | TRP151 |
| C | ASN186 |
| C | HOH3146 |
| C | HOH3350 |
| C | HOH3488 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 3002 |
| Chain | Residue |
| A | GLY240 |
| A | HIS241 |
| A | ASP458 |
| A | HOH3078 |
| A | HOH3169 |
| D | GLU526 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 3004 |
| Chain | Residue |
| B | ARG238 |
| B | GLY240 |
| B | HIS241 |
| B | ASP458 |
| B | HOH3081 |
| B | HOH3297 |
| C | GLU526 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 3005 |
| Chain | Residue |
| B | GLU526 |
| B | HOH3064 |
| B | HOH3215 |
| C | GLY240 |
| C | HIS241 |
| C | ASP458 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 3006 |
| Chain | Residue |
| A | ASP445 |
| A | PRO446 |
| A | ALA447 |
| A | TYR615 |
| A | LYS617 |
| A | HOH3194 |
| A | HOH3214 |
| A | HOH3313 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 3007 |
| Chain | Residue |
| A | GLU526 |
| D | GLY240 |
| D | HIS241 |
| D | ASP458 |
| D | HOH3013 |
| D | HOH3088 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 3008 |
| Chain | Residue |
| C | ASP445 |
| C | PRO446 |
| C | ALA447 |
| C | TYR615 |
| C | LYS617 |
| C | HOH3115 |
| C | HOH3143 |
| C | HOH3197 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 3009 |
| Chain | Residue |
| B | ASP445 |
| B | PRO446 |
| B | ALA447 |
| B | TYR615 |
| B | LYS617 |
| B | HOH3145 |
| B | HOH3154 |
| B | HOH3394 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 3010 |
| Chain | Residue |
| D | ASP445 |
| D | PRO446 |
| D | ALA447 |
| D | TYR615 |
| D | LYS617 |
| D | HOH3097 |
| D | HOH3266 |
| D | HOH3306 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 3011 |
| Chain | Residue |
| A | ARG55 |
| A | TRP151 |
| A | ASN186 |
| A | HOH3276 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12684501 |
| Chain | Residue | Details |
| A | TYR175 | |
| A | HIS340 | |
| A | SER174 | |
| A | TYR82 | |
| A | ASP307 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12684501 |
| Chain | Residue | Details |
| B | TYR175 | |
| B | HIS340 | |
| B | SER174 | |
| B | TYR82 | |
| B | ASP307 | |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12684501 |
| Chain | Residue | Details |
| C | TYR175 | |
| C | HIS340 | |
| C | SER174 | |
| C | TYR82 | |
| C | ASP307 | |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12684501 |
| Chain | Residue | Details |
| D | TYR175 | |
| D | HIS340 | |
| D | SER174 | |
| D | TYR82 | |
| D | ASP307 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 666 |
| Chain | Residue | Details |
| A | PRO94 | electrostatic stabiliser |
| A | SER198 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | PRO199 | electrostatic stabiliser |
| A | GLY351 | electrostatic stabiliser, increase basicity |
| A | ASN396 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 666 |
| Chain | Residue | Details |
| B | PRO94 | electrostatic stabiliser |
| B | SER198 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | PRO199 | electrostatic stabiliser |
| B | GLY351 | electrostatic stabiliser, increase basicity |
| B | ASN396 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 666 |
| Chain | Residue | Details |
| C | PRO94 | electrostatic stabiliser |
| C | SER198 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | PRO199 | electrostatic stabiliser |
| C | GLY351 | electrostatic stabiliser, increase basicity |
| C | ASN396 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 666 |
| Chain | Residue | Details |
| D | PRO94 | electrostatic stabiliser |
| D | SER198 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | PRO199 | electrostatic stabiliser |
| D | GLY351 | electrostatic stabiliser, increase basicity |
| D | ASN396 | proton acceptor, proton donor |
