6WI2
Structure of human mitochondrial complex Nfs1-ISCU2-ISD11 with E.coli ACP1 at 1.95 A resolution (NIAU)2. N-terminal mutation of ISCU2 (L35) traps Nfs1 Cys loop in the active site of ISCU2 without metal present.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0031071 | molecular_function | cysteine desulfurase activity |
A | 0044571 | biological_process | [2Fe-2S] cluster assembly |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0016226 | biological_process | iron-sulfur cluster assembly |
B | 0016604 | cellular_component | nuclear body |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0044571 | biological_process | [2Fe-2S] cluster assembly |
B | 0044572 | biological_process | [4Fe-4S] cluster assembly |
B | 0099128 | cellular_component | mitochondrial [2Fe-2S] assembly complex |
B | 1990221 | cellular_component | L-cysteine desulfurase complex |
B | 1990229 | cellular_component | iron-sulfur cluster assembly complex |
C | 0000035 | molecular_function | acyl binding |
C | 0000036 | molecular_function | acyl carrier activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0008289 | molecular_function | lipid binding |
C | 0008610 | biological_process | lipid biosynthetic process |
C | 0009245 | biological_process | lipid A biosynthetic process |
C | 0009410 | biological_process | response to xenobiotic stimulus |
C | 0031177 | molecular_function | phosphopantetheine binding |
D | 0005506 | molecular_function | iron ion binding |
D | 0016226 | biological_process | iron-sulfur cluster assembly |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue PLP A 501 |
Chain | Residue |
A | GLY126 |
A | HIS257 |
A | LYS258 |
A | THR295 |
A | HOH647 |
A | HOH726 |
A | ALA127 |
A | THR128 |
A | HIS156 |
A | MET203 |
A | ASP232 |
A | ALA234 |
A | GLN235 |
A | SER255 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | ARG321 |
A | THR415 |
A | GLU416 |
A | GLU417 |
B | ARG34 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | VAL173 |
A | THR174 |
A | TYR175 |
A | PEG527 |
A | HOH720 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | LYS431 |
A | ARG434 |
A | GLU435 |
A | TRP440 |
A | HOH630 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue PEG A 505 |
Chain | Residue |
A | ILE270 |
A | ARG271 |
A | ARG272 |
A | ARG275 |
A | VAL276 |
A | VAL278 |
A | MET291 |
A | HOH620 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue PEG A 506 |
Chain | Residue |
A | GLY115 |
A | ALA116 |
A | ASP117 |
A | PG4520 |
A | EDO528 |
A | HOH649 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | LEU69 |
A | TYR80 |
A | LEU81 |
A | PRO262 |
A | LYS263 |
A | PRO299 |
A | HOH613 |
A | HOH653 |
A | HOH707 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue GOL A 508 |
Chain | Residue |
A | PRO58 |
A | THR92 |
A | HIS93 |
A | ALA94 |
A | LEU367 |
A | MET368 |
A | LEU370 |
A | LYS371 |
A | EDO511 |
A | HOH779 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | MET368 |
A | ALA369 |
A | LYS371 |
A | HIS429 |
A | PEG539 |
D | VAL40 |
D | TYR43 |
D | GLU44 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO A 510 |
Chain | Residue |
A | MET334 |
A | LEU337 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue EDO A 511 |
Chain | Residue |
A | PRO58 |
A | TRP97 |
A | LYS371 |
A | GOL508 |
A | HOH639 |
A | HOH791 |
A | HOH844 |
D | LEU35 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 512 |
Chain | Residue |
A | LYS157 |
A | ARG164 |
A | PEG527 |
A | HOH690 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 513 |
Chain | Residue |
A | GLU104 |
A | ARG105 |
A | GLN108 |
A | HOH615 |
A | HOH632 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 514 |
Chain | Residue |
A | GLU100 |
A | ALA101 |
A | HOH615 |
A | HOH636 |
A | HOH811 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 515 |
Chain | Residue |
A | LYS248 |
A | ASP250 |
A | ARG271 |
A | HOH606 |
A | HOH702 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue EDO A 516 |
Chain | Residue |
A | SER125 |
A | SER125 |
A | ARG292 |
A | THR295 |
A | HOH647 |
A | HOH665 |
A | HOH665 |
A | HOH737 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue EDO A 517 |
Chain | Residue |
A | GLU316 |
A | HOH748 |
B | GLU42 |
B | EDO1605 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue EDO A 518 |
Chain | Residue |
A | GLN179 |
A | SER181 |
A | ILE183 |
A | ASP345 |
A | HOH601 |
A | HOH619 |
D | ASN45 |
D | HOH303 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue PEG A 519 |
Chain | Residue |
A | ASP75 |
A | HOH858 |
B | ARG68 |
B | LEU75 |
B | SER77 |
site_id | AE2 |
Number of Residues | 9 |
Details | binding site for residue PG4 A 520 |
Chain | Residue |
A | GLN108 |
A | SER112 |
A | ALA116 |
A | GLN312 |
A | GLN313 |
A | PEG506 |
A | HOH635 |
A | HOH649 |
A | HOH769 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue PG4 A 521 |
Chain | Residue |
A | ARG328 |
A | ASN332 |
A | ILE427 |
A | HOH741 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue PEG A 522 |
Chain | Residue |
A | PRO241 |
A | HIS319 |
site_id | AE5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 523 |
Chain | Residue |
A | ARG220 |
A | SER224 |
A | LYS248 |
D | ARG89 |
D | EDO203 |
site_id | AE6 |
Number of Residues | 2 |
Details | binding site for residue EDO A 524 |
Chain | Residue |
A | ARG119 |
A | ARG272 |
site_id | AE7 |
Number of Residues | 1 |
Details | binding site for residue EDO A 525 |
Chain | Residue |
A | GLN312 |
site_id | AE8 |
Number of Residues | 9 |
Details | binding site for residue ETE A 526 |
Chain | Residue |
A | LEU337 |
A | PRO338 |
A | ASP339 |
A | VAL340 |
A | TYR360 |
A | ASP400 |
A | LEU401 |
A | HOH756 |
A | HOH813 |
site_id | AE9 |
Number of Residues | 4 |
Details | binding site for residue PEG A 527 |
Chain | Residue |
A | GLN153 |
A | ARG164 |
A | EDO503 |
A | EDO512 |
site_id | AF1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 528 |
Chain | Residue |
A | GLN108 |
A | ASP117 |
A | PRO118 |
A | PEG506 |
site_id | AF2 |
Number of Residues | 4 |
Details | binding site for residue PEG A 529 |
Chain | Residue |
A | GLN331 |
A | MET342 |
A | HOH616 |
A | HOH786 |
site_id | AF3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 530 |
Chain | Residue |
A | GLU416 |
A | GLU417 |
A | ASP420 |
site_id | AF4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 531 |
Chain | Residue |
A | GLU217 |
A | HOH652 |
D | ARG47 |
D | ASN48 |
site_id | AF5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 532 |
Chain | Residue |
A | ASP420 |
A | TYR421 |
A | GLU424 |
A | HOH697 |
site_id | AF6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 534 |
Chain | Residue |
A | GLN428 |
A | ARG432 |
A | HOH661 |
A | HOH716 |
site_id | AF7 |
Number of Residues | 13 |
Details | binding site for residue PGE A 535 |
Chain | Residue |
A | ALA76 |
A | ARG105 |
A | GLN109 |
A | ALA306 |
A | GLU309 |
A | VAL310 |
A | GLN313 |
A | HOH607 |
A | HOH623 |
A | HOH681 |
A | HOH712 |
B | ARG61 |
B | HOH1755 |
site_id | AF8 |
Number of Residues | 2 |
Details | binding site for residue EDO A 536 |
Chain | Residue |
A | GLU314 |
B | ARG35 |
site_id | AF9 |
Number of Residues | 7 |
Details | binding site for residue PEG A 537 |
Chain | Residue |
A | ASP161 |
A | SER283 |
A | GLY284 |
A | GLY286 |
A | GLY290 |
A | HOH621 |
A | HOH772 |
site_id | AG1 |
Number of Residues | 8 |
Details | binding site for residue EDO A 538 |
Chain | Residue |
A | LYS212 |
A | PRO346 |
A | LYS347 |
A | HIS348 |
A | HIS349 |
A | HOH732 |
A | HOH806 |
A | HOH841 |
site_id | AG2 |
Number of Residues | 9 |
Details | binding site for residue PEG A 539 |
Chain | Residue |
A | GLN179 |
A | ASP185 |
A | LYS371 |
A | LYS425 |
A | GLN428 |
A | HIS429 |
A | ARG432 |
A | EDO509 |
D | GLU44 |
site_id | AG3 |
Number of Residues | 2 |
Details | binding site for residue PEG A 540 |
Chain | Residue |
A | HOH822 |
A | HOH856 |
site_id | AG4 |
Number of Residues | 7 |
Details | binding site for residue EDO B 1601 |
Chain | Residue |
A | PRO68 |
A | TYR85 |
A | PHE413 |
A | THR414 |
A | HOH682 |
B | ASN27 |
B | HOH1703 |
site_id | AG5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 1602 |
Chain | Residue |
A | ASP445 |
B | LEU12 |
site_id | AG6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 1603 |
Chain | Residue |
A | VAL443 |
A | GLN444 |
B | ARG61 |
B | HOH1716 |
site_id | AG7 |
Number of Residues | 4 |
Details | binding site for residue MES B 1604 |
Chain | Residue |
B | ARG41 |
B | LYS44 |
C | ASP35 |
C | ASP38 |
site_id | AG8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 1605 |
Chain | Residue |
A | EDO517 |
A | HOH774 |
B | HOH1708 |
B | HOH1736 |
B | HOH1751 |
site_id | AG9 |
Number of Residues | 3 |
Details | binding site for residue EDO B 1606 |
Chain | Residue |
A | ASP445 |
B | ARG67 |
B | PEG1607 |
site_id | AH1 |
Number of Residues | 5 |
Details | binding site for residue PEG B 1607 |
Chain | Residue |
B | ARG67 |
B | ARG68 |
B | LEU75 |
B | EDO1606 |
B | HOH1744 |
site_id | AH2 |
Number of Residues | 3 |
Details | binding site for residue EDO B 1608 |
Chain | Residue |
B | LYS21 |
B | PHE23 |
B | LYS80 |
site_id | AH3 |
Number of Residues | 5 |
Details | binding site for residue EDT B 1609 |
Chain | Residue |
A | GLU417 |
B | LYS21 |
B | ARG29 |
B | GLU84 |
B | HOH1721 |
site_id | AH4 |
Number of Residues | 12 |
Details | binding site for residue 8Q1 C 301 |
Chain | Residue |
B | ARG6 |
B | VAL9 |
B | ALA39 |
B | ASN43 |
B | LYS44 |
B | VAL46 |
B | HOH1735 |
C | ASP35 |
C | SER36 |
C | EDO302 |
C | HOH409 |
C | HOH413 |
site_id | AH5 |
Number of Residues | 4 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
C | VAL29 |
C | SER36 |
C | 8Q1301 |
C | HOH402 |
site_id | AH6 |
Number of Residues | 4 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | PRO55 |
C | TYR71 |
C | HIS75 |
D | LYS57 |
site_id | AH7 |
Number of Residues | 3 |
Details | binding site for residue EDO D 201 |
Chain | Residue |
D | GLN38 |
D | LYS127 |
D | GLU128 |
site_id | AH8 |
Number of Residues | 4 |
Details | binding site for residue EDO D 202 |
Chain | Residue |
A | GLU435 |
D | GLY50 |
D | LYS91 |
D | EDO203 |
site_id | AH9 |
Number of Residues | 6 |
Details | binding site for residue EDO D 203 |
Chain | Residue |
A | ARG220 |
A | EDO523 |
D | GLY50 |
D | SER51 |
D | ARG89 |
D | EDO202 |
site_id | AI1 |
Number of Residues | 5 |
Details | binding site for residue 1PE D 204 |
Chain | Residue |
D | GLY111 |
D | LYS112 |
D | GLU116 |
D | THR119 |
D | ILE120 |
site_id | AI2 |
Number of Residues | 5 |
Details | binding site for residue GOL D 205 |
Chain | Residue |
B | ARG14 |
B | HOH1727 |
C | ASP56 |
D | ASP53 |
D | THR55 |
site_id | AI3 |
Number of Residues | 3 |
Details | binding site for residue EDO D 206 |
Chain | Residue |
D | GLU107 |
D | TRP108 |
D | HOH321 |
Functional Information from PROSITE/UniProt
site_id | PS00012 |
Number of Residues | 16 |
Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL |
Chain | Residue | Details |
C | ASP31-LEU46 |
site_id | PS00595 |
Number of Residues | 20 |
Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDLMsiSGHKiygpk.GvGaI |
Chain | Residue | Details |
A | ILE249-ILE268 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Cysteine persulfide intermediate => ECO:0000250|UniProtKB:Q9D7P6 |
Chain | Residue | Details |
D | GLY94 | |
B | LYS44 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Cysteine persulfide intermediate => ECO:0000250|UniProtKB:O29689 |
Chain | Residue | Details |
D | GLU163 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31101807, ECO:0007744|PDB:6NZU |
Chain | Residue | Details |
D | GLY96 | |
D | ILE120 | |
D | GLU163 | |
A | HIS257 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Mediates ISCU dimerization and de novo [2Fe-2S] cluster assembly => ECO:0000269|PubMed:34824239 |
Chain | Residue | Details |
D | GLY60 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by MTOR => ECO:0000269|PubMed:23508953 |
Chain | Residue | Details |
D | VAL39 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine persulfide => ECO:0000250|UniProtKB:Q9D7P6 |
Chain | Residue | Details |
D | GLY94 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine persulfide => ECO:0000305|PubMed:24971490 |
Chain | Residue | Details |
D | GLU163 |