9dhw

Q23.MD39 in Complex with Fabs from antibodies CH01 iGL and 35O22

Method: ELECTRON MICROSCOPY D_max: 164.6 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Q23.MD39 Surface protein gp120

Human immunodeficiency virus 1

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 12 其他Polymer 28 PDB declaration: 12-meric（12） Consistent with protein copy count	Chain A； UniProt 31–497 Chain B； UniProt 502–654 Chain C； UniProt 31–497 Chain D； UniProt 502–654 Chain G； UniProt 31–497 Chain I； UniProt 502–654	Not recorded	35O22 Fab Heavy Chain × 2 35O22 Fab Light Chain × 2 CH01 iGL Fab Light Chain × 1 CH01 iGL Fab Heavy Chain × 1 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 22	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6；1X PBS cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 9DHW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4YDI Crystal structure of broad and potently neutralizing VRC01-class antibody Z258-VRC27.01, isolated from human donor Z258, in complex with HIV-1 gp120 from clade A strain Q23.17 Deposited 2015-02-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 43–122（80 aa） Fragment：UNP residues 43-122, 191-293, 315-482 Chain G 191–293（103 aa） Fragment：UNP residues 43-122, 191-293, 315-482 Chain G 315–482（168 aa） Fragment：UNP residues 43-122, 191-293, 315-482	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 SO4 SULFATE ION × 4 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；4% PEG 400, 1.9 M (NH4)2SO4, 0.1M Tris-HCl, pH 8.5	Resolution 3.45 Å R-free 0.276
7LLK Cryo-EM structure of Q23.17_DS-SOSIP in complex with Glycan276-Dependent Broadly Neutralizing Antibody 179NC75 Fab Deposited 2021-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 31–498（468 aa） Chain E 31–498（468 aa） Chain I 31–498（468 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；Blot for 2.5 S before plunging	Resolution 4.80 Å
9BNL Cryo-EM structure of rhesus antibody 6070-a.01 in complex with HIV-1 Env trimer Q23.17 MD39 Deposited 2024-05-02	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain A 32–495（464 aa） Chain B 510–651（142 aa） Chain C 32–495（464 aa） Chain E 32–495（464 aa） Chain F 510–651（142 aa） Chain G 510–651（142 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9BTV Cryo-EM structure of rhesus antibody T646-a.01 in complex with HIV-1 Env trimer Q23.17 MD39 Deposited 2024-05-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain A 30–498（469 aa） Chain B 502–654（153 aa） Chain C 30–498（469 aa） Chain E 30–498（469 aa） Chain F 502–654（153 aa） Chain G 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.48 Å
9DIM Q23.MD39 in Complex with Fab from antibody 35O22 Deposited 2024-09-05	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 31–497（467 aa） Chain B 502–654（153 aa） Chain C 31–497（467 aa） Chain D 502–654（153 aa） Chain G 31–497（467 aa） Chain I 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；1X PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.19 Å
9NVV Cryo-EM structure of V2 apex germline-targeting HIV Env trimer Q23-APEX-GT2 Deposited 2025-03-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 6 PDB declaration: hexameric	Chain b 30–584（555 aa） Chain c 502–654（153 aa） Chain d 30–584（555 aa） Chain e 502–654（153 aa） Chain f 30–584（555 aa） Chain g 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 32	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9NVW Cryo-EM structure of rhesus antibody CH35-Apex1.08 in complex with HIV Env trimer Q23-APEX-GT2 Deposited 2025-03-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–507（478 aa） Chain c 502–654（153 aa） Chain d 30–507（478 aa） Chain e 502–654（153 aa） Chain f 30–507（478 aa） Chain g 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 32	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9NVX Cryo-EM structure of rhesus antibody CI91-Apex1.01 in complex with HIV Env trimer Q23-APEX-GT2 Deposited 2025-03-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–507（478 aa） Chain c 502–654（153 aa） Chain d 30–507（478 aa） Chain e 502–654（153 aa） Chain f 30–507（478 aa） Chain g 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 31	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9NVY Cryo-EM structure of rhesus antibody CH70-Apex2.01 in complex with HIV Env trimer Q23-APEX-GT2 Deposited 2025-03-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–507（478 aa） Chain c 502–654（153 aa） Chain d 30–507（478 aa） Chain e 502–654（153 aa） Chain f 30–507（478 aa） Chain g 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 32	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9NVZ Cryo-EM structure of rhesus antibody CH70-Apex1.01 in complex with HIV Env trimer Q23-APEX-GT2 Deposited 2025-03-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–507（478 aa） Chain c 502–654（153 aa） Chain d 30–507（478 aa） Chain e 502–654（153 aa） Chain f 30–507（478 aa） Chain g 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 27	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9NW0 Cryo-EM structure of rhesus antibody CH42-Apex1.01 in complex with HIV Env trimer Q23-APEX-GT2 Deposited 2025-03-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–507（478 aa） Chain c 502–654（153 aa） Chain d 30–507（478 aa） Chain e 502–654（153 aa） Chain f 30–507（478 aa） Chain g 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
9NW1 Cryo-EM structure of rhesus antibody CH42-Apex2.01 in complex with HIV Env trimer Q23-APEX-GT2 Deposited 2025-03-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–507（478 aa） Chain c 502–654（153 aa） Chain d 30–507（478 aa） Chain e 502–654（153 aa） Chain f 30–507（478 aa） Chain g 502–654（153 aa）	Not recorded	MAN alpha-D-mannopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 28	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9Z9L Q23.MD39 in Complex with Fabs from antibodies CH01 and 35O22 Deposited 2025-11-18	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 31–497（467 aa） Chain B 502–654（153 aa） Chain C 31–497（467 aa） Chain D 502–654（153 aa） Chain G 31–497（467 aa） Chain I 502–654（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；1X PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.49 Å
9ZRX Cryo-EM structure of SHIV-elicited CE79-1571 Fab in complex with HIV Env trimer Q23-SCT27 Deposited 2025-12-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–497（468 aa） Chain c 502–654（153 aa） Chain d 30–497（468 aa） Chain e 502–654（153 aa） Chain f 30–497（468 aa） Chain g 502–654（153 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 3.30 Å
9ZRY Cryo-EM structure of SHIV-elicited CN81-2029 Fab in complex with HIV Env trimer Q23-SCT27 Deposited 2025-12-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–497（468 aa） Chain c 502–654（153 aa） Chain d 30–497（468 aa） Chain e 502–654（153 aa） Chain f 30–497（468 aa） Chain g 502–654（153 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 2.90 Å
9ZRZ Cryo-EM structure of SHIV-elicited CI93-1365 Fab in complex with HIV Env trimer Q23-SCT27 Deposited 2025-12-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain b 30–497（468 aa） Chain c 502–654（153 aa） Chain d 30–497（468 aa） Chain e 502–654（153 aa） Chain f 30–497（468 aa） Chain g 502–654（153 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY mmCIF provides none of the parsed conditions	Resolution 2.90 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	O55774_9HIV1
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–467； UniProt 31–497 Author chain C； PDBConstruct 1–467； UniProt 31–497 Author chain G； PDBConstruct 1–467； UniProt 31–497 Author chain B； PDBConstruct 1–153； UniProt 502–654 Author chain D； PDBConstruct 1–153； UniProt 502–654 Author chain I； PDBConstruct 1–153； UniProt 502–654

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9dhw
Deposition date deposition_date	2024-09-04
Structure title title	Q23.MD39 in Complex with Fabs from antibodies CH01 iGL and 35O22
Keywords keywords	Antibody, Complex, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	50.29 Å
Radius of gyration Rg (electron density) rg_electron	50.01 Å
Forward intensity I(0) i0	1255090000.00
Molecular weight molecular_weight	290620.0 kDa
Excluded volume excluded_volume	362000 Å³
Envelope volume envelope_volume	515550 Å³
Hydration-shell volume shell_volume	86133 Å³
Envelope diameter envelope_diameter	178.7 Å
Shell Rg shell_rg	53.30 Å
Envelope Rg envelope_rg	49.51 Å
Shape Rg shape_rg	50.02 Å
Total Rg total_rg	50.09 Å
Total atoms total_atoms	20383
Residues n_residues	2407
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	164.6 Å
Rg (real space) rg_real	50.26 Å
Rg uncertainty (real space) rg_real_error	1.46 Å
I(0) (real space) i0_real	1.2550e+09
I(0) uncertainty (real space) i0_real_error	2.3770e+07
Rg (reciprocal space) rg_reciprocal	50.31 Å
I(0) (reciprocal space) i0_reciprocal	1255000000.0000
Solution quality estimate total_estimate	0.8659
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	63.7 Å
Skewness Skewness skewness	0.325
Kurtosis Kurtosis kurtosis	-0.195
Angular range angular_range	— – 0.1550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	80850000.0000
Real-space data points n_real_points	32
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.649

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (16)

Entity 1 Entity 1 polymer

Description description	Q23.MD39 Surface protein gp120
Molecular weight formula_weight	52753.8 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,G
Atom count atom_count	20383

ENLWVTVYYGVPVWRDADTTLFCASDAKAYETEKHNVWATHACVPTDPNPQEIHLDNVTEKFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTSVNTTGDREGLKNCSFNMTTELRDKRQKVYSLFYRLDIVPINENQGSEYRLINCNTSAITQACPKVSFEPIPIHYCTPAGFAILKCKDEGFNGTGLCKNVSTVQCTHGIKPVVSTQLLLNGSLAEKNIIIRSENITNNAKIIIVQLVQPVTIKCIRPNNNTVKSIRIGPGQAFYYTGDIIGDIRQAHCNVTRSRWNKTLQEVAEKLRTYFGNKTIIFAQSSGGDLEITTHSFNCGGEFFYCNTSGLFNSTWYVNSTWNDTDSTQESNDTITLPCRIKQIINMWQRAGQAMYAPPIPGVIKCESNITGLLLTRDGGKDNNVNETFRPGGSDMRDNWRSELYKYKVVEIEPLGVAPTRCKRRVVE

来源 Source

来源生物 organism	Human immunodeficiency virus 1
NCBI Class编号 ncbi_taxonomy_id	11676
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Q23.MD39 Transmembrane protein gp41
Molecular weight formula_weight	17329.6 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,I

AVGIGAVSLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQNNLLRAPEPQQHLLKDTHWGIKQLQARVLAVEHYLRDQQLLGIWGCSGKLICCTNVPWNSSWSNKSLDEIWNNMTWLQWDKEINNYTQLIYRLIEESQNQQEKNEKELLELD

来源 Source

来源生物 organism	Human immunodeficiency virus 1
NCBI Class编号 ncbi_taxonomy_id	11676
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	35O22 Fab Heavy Chain
Molecular weight formula_weight	26170.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,H

QGQLVQSGAELKKPGASVKISCKTSGYRFNFYHINWIRQTAGRGPEWMGWISPYSGDKNLAPAFQDRVIMTTDTEVPVTSFTSTGAAYMEIRNLKFDDTGTYFCAKGLLRDGSSTWLPYLWGQGTLLTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKGLEVLFQ

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 4 Entity 4 polymer

Description description	35O22 Fab Light Chain
Molecular weight formula_weight	23318.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,L

QSVLTQSASVSGSLGQSVTISCTGPNSVCCSHKSISWYQWPPGRAPTLIIYEDNERAPGISPRFSGYKSYWSAYLTISDLRPEDETTYYCCSYTHNSGCVFGTGTKVSVLGQSKANPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 5 Entity 5 polymer

Description description	CH01 iGL Fab Light Chain
Molecular weight formula_weight	11663.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M

EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPYTFGQGTKVEIK

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 6 Entity 6 polymer

Description description	CH01 iGL Fab Heavy Chain
Molecular weight formula_weight	14541.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N

EVQLVESGGGVVRPGGSLRLSCAASGFTFDDYGMSWVRQAPGKGLEWVSGINWNGGSTGYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTALYHCARGTDYTIDDQGIHYYGSGTYWYFDLWGRGTLVTVSS

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 7 Entity 7 branched

Description description	;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	1073.0 kDa
Source method src_method	man
Copy count entity_count	1

Entity 8 Entity 8 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	16

Entity 9 Entity 9 branched

Description description	;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	1235.1 kDa
Source method src_method	man
Copy count entity_count	1

Entity 10 Entity 10 branched

Description description	beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	586.5 kDa
Source method src_method	man
Copy count entity_count	4

Entity 11 Entity 11 branched

Description description	alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	367.3 kDa
Source method src_method	man
Copy count entity_count	1

Entity 12 Entity 12 branched

Description description	;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	910.8 kDa
Source method src_method	man
Copy count entity_count	1

Entity 13 Entity 13 branched

Description description	;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	910.8 kDa
Source method src_method	man
Copy count entity_count	2

Entity 14 Entity 14 branched

Description description	;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	1397.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 15 Entity 15 branched

Description description	;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	732.7 kDa
Source method src_method	man
Copy count entity_count	1

Entity 16 Entity 16 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	22

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8. Citations (2)

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Resolution resolution	3.35 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	71949

fit	/app/data/saxs_computation/dh/9dhw/9dhw.fit
pddf	/app/data/pr_computation/dh/9dhw/9dhw.pr.out
profile	/app/data/saxs_computation/dh/9dhw/9dhw.dat

Q23.MD39 in Complex with Fabs from antibodies CH01 iGL and 35O22

1. Protein Identity and Related Structures Protein Identity & Related Structures

Q23.MD39 Surface protein gp120

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (16)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 polymer

Polymer Polymer

来源 Source

Entity 6 Entity 6 polymer

Polymer Polymer

来源 Source

Entity 7 Entity 7 branched

Entity 8 Entity 8 branched

Entity 9 Entity 9 branched

Entity 10 Entity 10 branched

Entity 11 Entity 11 branched

Entity 12 Entity 12 branched

Entity 13 Entity 13 branched

Entity 14 Entity 14 branched

Entity 15 Entity 15 branched

Entity 16 Entity 16 non-polymer

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)