1F0V
Crystal structure of an Rnase A dimer displaying a new type of 3D domain swapping
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 | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 801 |
| Chain | Residue |
| A | GLN11 |
| A | HIS12 |
| A | LYS41 |
| A | HOH1004 |
| A | HOH1252 |
| A | HOH1553 |
| B | HIS319 |
| B | PHE320 |
| M | DG752 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 802 |
| Chain | Residue |
| A | HIS119 |
| A | PHE120 |
| B | GLN211 |
| B | HIS212 |
| B | LYS241 |
| B | HOH1074 |
| B | HOH1396 |
| B | HOH1554 |
| B | HOH1555 |
| N | DG754 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 C 803 |
| Chain | Residue |
| C | GLN411 |
| C | HIS412 |
| C | LYS441 |
| C | HOH1045 |
| C | HOH1571 |
| D | HIS719 |
| D | PHE720 |
| O | DG756 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 P 804 |
| Chain | Residue |
| C | HIS519 |
| C | PHE520 |
| D | GLN611 |
| D | HIS612 |
| D | LYS641 |
| P | DG758 |
| P | HOH1029 |
| P | HOH1273 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 901 |
| Chain | Residue |
| C | ALA405 |
| C | GLU511 |
| D | ASN713 |
| D | PRO714 |
| D | HOH1051 |
| D | HOH1254 |
| D | HOH1355 |
| D | HOH1575 |
| D | HOH1576 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 902 |
| Chain | Residue |
| B | GLN301 |
| B | ALA302 |
| B | ASN303 |
| B | HOH1442 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 903 |
| Chain | Residue |
| C | PRO442 |
| C | HOH1179 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 904 |
| Chain | Residue |
| A | GLN69 |
| A | THR70 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 905 |
| Chain | Residue |
| B | GLU202 |
| B | ALA206 |
| B | GLU209 |
| B | ARG210 |
| B | GOL922 |
| B | HOH1307 |
| B | HOH1514 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 906 |
| Chain | Residue |
| B | SER223 |
| B | THR299 |
| B | THR300 |
| B | GLN301 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 907 |
| Chain | Residue |
| A | VAL124 |
| B | VAL263 |
| B | ALA264 |
| B | GLN274 |
| B | ILE307 |
| B | HOH1192 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 908 |
| Chain | Residue |
| A | SER50 |
| A | ALA52 |
| A | ASP53 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 909 |
| Chain | Residue |
| D | GLU711 |
| D | GLY712 |
| D | ASN713 |
| D | HOH1303 |
| D | HOH1581 |
| D | HOH1582 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 910 |
| Chain | Residue |
| A | ASN113 |
| A | PRO114 |
| A | VAL116 |
| B | GLU311 |
| B | GLY312 |
| B | ASN313 |
| B | GOL920 |
| B | HOH1056 |
| B | HOH1123 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 911 |
| Chain | Residue |
| C | ASN503 |
| C | GOL912 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 912 |
| Chain | Residue |
| A | THR78 |
| A | GOL911 |
| C | THR478 |
| C | ASN503 |
| C | HOH1157 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 913 |
| Chain | Residue |
| D | GLN701 |
| D | ALA702 |
| D | ASN703 |
| D | HOH1509 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 914 |
| Chain | Residue |
| B | CYS240 |
| B | LYS241 |
| B | PRO242 |
| B | ARG239 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 915 |
| Chain | Residue |
| A | ARG39 |
| A | PRO42 |
| A | HOH1330 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 916 |
| Chain | Residue |
| D | SER623 |
| D | THR699 |
| D | THR700 |
| D | GLN701 |
| D | HOH1281 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 917 |
| Chain | Residue |
| C | SER422 |
| C | THR499 |
| C | THR500 |
| C | GLN501 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 918 |
| Chain | Residue |
| A | SER23 |
| A | THR99 |
| A | HOH1062 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 919 |
| Chain | Residue |
| C | SER450 |
| C | ASP453 |
| C | HOH1437 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 920 |
| Chain | Residue |
| B | ALA204 |
| B | GLU311 |
| B | ASN313 |
| B | GOL910 |
| B | HOH1332 |
| B | HOH1494 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 921 |
| Chain | Residue |
| B | ALA256 |
| B | SER259 |
| B | GLN260 |
| B | HOH1010 |
| B | HOH1348 |
| B | HOH1431 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 922 |
| Chain | Residue |
| B | GLU202 |
| B | ARG210 |
| B | ASN234 |
| B | GOL905 |
| B | HOH1269 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 923 |
| Chain | Residue |
| A | SER77 |
| A | HOH1140 |
| A | HOH1579 |
| C | THR478 |
| C | HIS505 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 924 |
| Chain | Residue |
| D | ASP653 |
| D | ALA656 |
| D | HOH1021 |
| D | HOH1028 |
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 |
