Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0003676 | molecular_function | nucleic acid binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 101 |
Chain | Residue |
A | LYS7 |
A | GLN11 |
A | HOH218 |
B | ARG39 |
B | HOH337 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 102 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 103 |
Chain | Residue |
B | ASN34 |
B | ARG39 |
A | ARG10 |
A | GLN11 |
A | HOH218 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 104 |
Chain | Residue |
A | SER15 |
A | HOH216 |
B | LEU51 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 201 |
Chain | Residue |
A | GLN11 |
A | HIS12 |
B | HIS119 |
B | PHE120 |
B | HOH317 |
B | HOH337 |
B | HOH395 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 202 |
Chain | Residue |
B | ASP83 |
B | ALA122 |
B | VAL124 |
B | HOH397 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 203 |
Chain | Residue |
B | PRO42 |
B | VAL43 |
B | HOH363 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 204 |
Chain | Residue |
A | HIS12 |
B | THR45 |
B | HOH395 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 205 |
Chain | Residue |
B | GLN69 |
B | THR70 |
B | ASN71 |
B | TYR115 |
B | HOH403 |
B | HOH403 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 206 |
Chain | Residue |
B | ASN71 |
B | HIS119 |
B | HOH390 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 207 |
Chain | Residue |
B | ARG39 |
B | CYS40 |
B | HOH306 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 208 |
Chain | Residue |
B | ALA102 |
B | ASN103 |
B | HOH404 |
B | HOH409 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 209 |
Chain | Residue |
B | GLN28 |
B | ARG39 |
B | PRO42 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 210 |
Chain | Residue |
B | CYS65 |
B | LYS66 |
B | ARG85 |
B | ASP121 |
Functional Information from PROSITE/UniProt
site_id | PS00127 |
Number of Residues | 7 |
Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF |
Chain | Residue | Details |
B | CYS40-PHE46 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
B | HIS119 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
B | LYS41 | |
B | LYS66 | |
B | ARG85 | |
Chain | Residue | Details |
B | ASN34 | |
A | LYS7 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 |
Chain | Residue | Details |
B | LYS37 | |
B | LYS41 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 164 |
Chain | Residue | Details |
B | LYS41 | electrostatic stabiliser, hydrogen bond donor |
B | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | PHE120 | electrostatic stabiliser, hydrogen bond donor |
B | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |