HIV-1 HXBC2 GP120 envelope glycoprotein complexed with CD4 and induced neutralizing antibody 17B. Determined by X-ray diffraction at 2.2 Å resolution. Released 3 Feb 2004.
Explore 1RZJ in 3D Show helices and sheets RCSB PDB PDBe
1RZJ contains 30 α-helices and 90 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 7 |
| β-strand | 12-14 | 3 | 8 |
| β-strand | 17 | 1 | 9 |
| β-strand | 26-30 | 5 | 7 |
| β-strand | 35-40 | 6 | 7 |
| β-strand | 43-46 | 4 | 7 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 8 |
| α-helix | 62-64 | 3 | |
| β-strand | 66 | 1 | 9 |
| β-strand | 69-71 | 3 | 8 |
| β-strand | 80-86 | 7 | 7 |
| β-strand | 89-98 | 10 | 7 |
| β-strand | 99-102 | 4 | 10 |
| β-strand | 108-109 | 2 | 11 |
| β-strand | 114-119 | 6 | 10 |
| α-helix | 126 | 1 | |
| β-strand | 127-131 | 5 | 12 |
| β-strand | 137-140 | 4 | 12 |
| β-strand | 143-146 | 4 | 10 |
| α-helix | 151-153 | 3 | |
| β-strand | 155-163 | 9 | 12 |
| β-strand | 166-174 | 9 | 12 |
| β-strand | 176-177 | 2 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 84-93 | 10 | 1 |
| α-helix | 95-97 | 3 | |
| α-helix | 99-113 | 15 | |
| β-strand | 120-123 | 4 | 2 |
| β-strand | 199-202 | 4 | 2 |
| α-helix | 212-214 | 3 | |
| β-strand | 215 | 1 | 3 |
| β-strand | 218 | 1 | 4 |
| α-helix | 219-220 | 2 | |
| β-strand | 223-228 | 6 | 1 |
| β-strand | 237-245 | 9 | 1 |
| β-strand | 247 | 1 | 4 |
| α-helix | 248-250 | 3 | |
| β-strand | 251 | 1 | 3 |
| β-strand | 256 | 1 | 5 |
| β-strand | 259-261 | 3 | 6 |
| β-strand | 271-273 | 3 | 6 |
| β-strand | 284-297 | 14 | 6 |
| β-strand | 330-334 | 5 | 6 |
| α-helix | 335-352 | 18 | |
| β-strand | 358-361 | 4 | 6 |
| β-strand | 367 | 1 | 7 |
| α-helix | 369-372 | 4 | |
| β-strand | 374-378 | 5 | 5 |
| β-strand | 381-385 | 5 | 5 |
| α-helix | 388-390 | 3 | |
| β-strand | 393-395 | 3 | 6 |
| β-strand | 413-417 | 5 | 6 |
| β-strand | 420-421 | 2 | 5 |
| β-strand | 423-425 | 3 | 2 |
| β-strand | 432-434 | 3 | 2 |
| α-helix | 436-438 | 3 | |
| β-strand | 444-456 | 13 | 6 |
| β-strand | 465-470 | 6 | 6 |
| α-helix | 475-483 | 9 | |
| β-strand | 486-490 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 18 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 19 |
| β-strand | 18-25 | 8 | 18 |
| α-helix | 29-31 | 3 | |
| β-strand | 32-39 | 8 | 19 |
| β-strand | 46-52 | 7 | 19 |
| β-strand | 56-59 | 4 | 19 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 18 |
| β-strand | 77-82 | 6 | 18 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 19 |
| α-helix | 100-100B | 3 | |
| β-strand | 102-103 | 2 | 19 |
| β-strand | 104 | 1 | 18 |
| β-strand | 107-111 | 5 | 19 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 20 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 21 |
| β-strand | 135-145 | 11 | 21 |
| β-strand | 146 | 1 | 20 |
| β-strand | 151-154 | 4 | 22 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 22 |
| β-strand | 163-165 | 3 | 21 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 21 |
| β-strand | 176-185 | 10 | 21 |
| α-helix | 186-188 | 3 | |
| β-strand | 195-200 | 6 | 22 |
| β-strand | 205-210 | 6 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 13 |
| β-strand | 10-13 | 4 | 14 |
| β-strand | 19-25 | 7 | 13 |
| β-strand | 33-38 | 6 | 14 |
| β-strand | 45-49 | 5 | 14 |
| β-strand | 53-54 | 2 | 14 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 13 |
| β-strand | 70-75 | 6 | 13 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 14 |
| β-strand | 97-98 | 2 | 14 |
| β-strand | 102-106 | 5 | 14 |
| β-strand | 111 | 1 | 15 |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 130-139 | 10 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 145-150 | 6 | 17 |
| β-strand | 153-154 | 2 | 17 |
| β-strand | 159-163 | 5 | 16 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-181 | 9 | 16 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 17 |
| β-strand | 205-210 | 6 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Envelope glycoprotein GP120 | G | protein | 321 | Human immunodeficiency virus 1 | P04578 (AlphaFold model) |
| T-cell surface glycoprotein CD4 | C | protein | 185 | Homo sapiens | P01730 (AlphaFold model) |
| Antibody 17B, light chain | L | protein | 214 | Homo sapiens | |
| Antibody 17B, heavy chain | H | protein | 229 | Homo sapiens |
>1RZJ_1 ENVELOPE GLYCOPROTEIN GP120 (chains G) GARSEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVGAGSCNTSVIT QACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLN GSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTGAGHCNISRAKWNNTLKQIASKLRE QFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGS DTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPG GGDMRDNWRSELYKYKVVKIE
>1RZJ_2 T-CELL SURFACE GLYCOPROTEIN CD4 (chains C) KKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRS LWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLES PPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQ KASNT
>1RZJ_3 ANTIBODY 17B, LIGHT CHAIN (chains L) DIVMTQSPATLSVSPGERATLSCRASESVSSDLAWYQQKPGQAPRLLIYGASTRATGVPA RFSGSGSGAEFTLTISSLQSEDFAVYYCQQYNNWPPRYTFGQGTRLEIKRTVAAPSVFIF PPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSST LTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
>1RZJ_4 ANTIBODY 17B, HEAVY CHAIN (chains H) EVQLVESGAEVKKPGSSVKVSCKASGDTFIRYSFTWVRQAPGQGLEWMGRIITILDVAHY APHLQGRVTITADKSTSTVYLELRNLRSDDTAVYFCAGVYEGEADEGEYDNNGFLKHWGQ GTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHT FPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 12 |
| IPA | Isopropyl alcohol | C3 H8 O | 1 |
Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120. Huang, C.C., Venturi, M., Majeed, S. et al. Proc Natl Acad Sci U S A (2004) 101:2706-2711. DOI 10.1073/pnas.0308527100 · PubMed
Other PDB entries of the same protein (UniProt P04578 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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