1BZQ
COMPLEX OF A DROMEDARY SINGLE-DOMAIN VHH ANTIBODY FRAGMENT WITH RNASE A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004522 | molecular_function | ribonuclease A activity |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0016829 | molecular_function | lyase activity |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004522 | molecular_function | ribonuclease A activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016829 | molecular_function | lyase activity |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0004522 | molecular_function | ribonuclease A activity |
| C | 0004540 | molecular_function | RNA nuclease activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0016829 | molecular_function | lyase activity |
| C | 0050830 | biological_process | defense response to Gram-positive bacterium |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0004522 | molecular_function | ribonuclease A activity |
| D | 0004540 | molecular_function | RNA nuclease activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0016829 | molecular_function | lyase activity |
| D | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
| Chain | Residue |
| A | LYS7 |
| A | GLN11 |
| A | HIS12 |
| A | HIS119 |
| A | PHE120 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2002 |
| Chain | Residue |
| B | PHE320 |
| B | GLN211 |
| B | HIS212 |
| B | LYS241 |
| B | HIS319 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 2003 |
| Chain | Residue |
| C | GLN411 |
| C | HIS412 |
| C | HIS519 |
| C | PHE520 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 2004 |
| Chain | Residue |
| D | GLN611 |
| D | HIS612 |
| D | LYS641 |
| D | HIS719 |
| D | PHE720 |
Functional Information from PROSITE/UniProt
| site_id | PS00127 |
| Number of Residues | 7 |
| Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF |
| Chain | Residue | Details |
| A | CYS40-PHE46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS12 | |
| B | HIS212 | |
| C | HIS412 | |
| D | HIS612 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS119 | |
| B | HIS319 | |
| C | HIS519 | |
| D | HIS719 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS7 | |
| B | ARG285 | |
| C | LYS407 | |
| C | ARG410 | |
| C | LYS441 | |
| C | LYS466 | |
| C | ARG485 | |
| D | LYS607 | |
| D | ARG610 | |
| D | LYS641 | |
| D | LYS666 | |
| A | ARG10 | |
| D | ARG685 | |
| A | LYS41 | |
| A | LYS66 | |
| A | ARG85 | |
| B | LYS207 | |
| B | ARG210 | |
| B | LYS241 | |
| B | LYS266 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 |
| Chain | Residue | Details |
| A | LYS1 | |
| C | LYS407 | |
| C | LYS437 | |
| C | LYS441 | |
| D | LYS601 | |
| D | LYS607 | |
| D | LYS637 | |
| D | LYS641 | |
| A | LYS7 | |
| A | LYS37 | |
| A | LYS41 | |
| B | LYS201 | |
| B | LYS207 | |
| B | LYS237 | |
| B | LYS241 | |
| C | LYS401 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
| Chain | Residue | Details |
| A | ASN34 | |
| B | ASN234 | |
| C | ASN434 | |
| D | ASN634 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| A | PHE120 | |
| A | HIS119 | |
| A | HIS12 | |
| A | LYS41 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| B | HIS212 | |
| B | HIS319 | |
| B | PHE320 | |
| B | LYS241 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| C | LYS441 | |
| C | PHE520 | |
| C | HIS519 | |
| C | HIS412 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| D | LYS641 | |
| D | HIS719 | |
| D | HIS612 | |
| D | PHE720 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| A | HIS119 | |
| A | HIS12 | |
| A | LYS41 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| B | HIS212 | |
| B | HIS319 | |
| B | LYS241 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| C | LYS441 | |
| C | HIS519 | |
| C | HIS412 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| D | LYS641 | |
| D | HIS719 | |
| D | HIS612 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| A | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | PHE120 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| B | HIS212 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS241 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS319 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | PHE320 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP321 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| C | HIS412 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | LYS441 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS519 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | PHE520 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP521 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| D | HIS612 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | LYS641 | electrostatic stabiliser, hydrogen bond donor |
| D | HIS719 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | PHE720 | electrostatic stabiliser, hydrogen bond donor |
| D | ASP721 | electrostatic stabiliser, hydrogen bond acceptor |
